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3. Effect of Total Apple Polyphenols Extract as Inhibitors of Amyloid Protein Aggregation

Author

Guarrasi, V, Rappa, C, COSTA, Maria Ambra, Librizzi, F, Raimondo, M, Vilasi, S, Bulone, D, San Biagio, PL, Germana, M, Guarrasi, V, Rappa, C, Costa, MA, Librizzi, F, Raimondo, M, Vilasi, S, Bulone, D, San Biagio, PL, and Germana, M

Abstract

Effect of Total Apple Polyphenols Extract as Inhibitors of Amyloid Protein Aggregation By: Guarrasi, Valeria; Rappa, Cinzia Giacoma; Costa, Maria Assunta; et al. JOURNAL OF CLINICAL GASTROENTEROLOGY Volume: 52 Supplement: 1 Pages: S94-S94 Published: NOV-DEC 2018

Published
2018

9. Contributory presentations/posters

Author

Gries, A., Singh, Balwinder, Nakazawal, Chicko, Genest, D., Getzoff, E. D., Matsuo, H., Kaur, Harpreet, Borst, J. W., Chadha, K. C., Tingyun, Kuang, Jagannadham, M. V., Leijon, Mikael, Sato, S., Bhakuni, Vlnod, Vijayan, M., Surolia, A., Suguna, K., Manoj, N., Srinivas, V. R., Ravishankar, R., Laggner, P., Prassl, R., Schwarzenbacher, R., Zeth, K., Kostner, G. M., Taylor, Susan S., Xuong, Nguyen-huu, Akamine, Pearl, Sagar, Bidva M., Saikrishnan, K., Purnapatre, K., Handa, P., Roy, S., Varshney, U., Biswal, B. K., Sukumar, N., Rao, J. K. Mohana, Johnson, A., Pattabhi, Vasantha, Murthy, M. R. N., Krishna, Sri S., Savithri, H. S., Sastri, Mira, Hosur, M. V., Pillai, Bindu, Kannan, K. K., Kumar, Mukesh, Patwardhan, Swati, Padmanabhaa, B., Sasaki-Sugio, S., Matsuzaki, T., Nukaga, M., Singh, T. P., Sharma, A. K., Srinivasan, A., Khan, J. A., Paramasivam, M., Kumar, P., Karthikevan, S., Sharma, S., Yadav, S., Srintvasan, A., Alam, Neelima, Gourinath, S., Kaur, Punit, Chandra, Vikas, Betzel, Ch., Ghosh, S., Bera, A. K., Pal, A. K., Baneriee, Asok, Mukhopadhyay, B. P., Bhattacharya, S., Chakraborty, S., Haldar, U., Dey, I., Solovicova, Adriana, Sevcik, Jozef, Sekar, K., Sundaralingam, M., Genov, N., Liang, Dong-cai, Zhang, Ji-ping, Jiang, Tao, Chang, Wen-rui, Blommers, Marcel, Jahnke, Wolfgang, Hosur, R. V., Panchal, S. C., Pillay, Bindu, Jaganathan, N. R., Mathur, Puniti, Srivatsun, S., Joshi, Ratan Mani, Chauhan, V. S., Govil, Girjesh, Atreya, H. S., Sahu, S. C., Quinjou, Éric, Adjadj, Elisabeth, Mispelter, Joël, Izadi-Pruneyre, Nadia, Blouquit, Yves, Heyd, Bernadette, Lerat, Guilhem, Desmadreil, Michel, Milnard, Philippe, Lin, Y., Rao, B. D. Nageswara, Raghunathan, Vidva, Chau, Mei H., Coutinho, Evans, Pesais, Prashant, Srivastava, Sudha, Saran, Anil, Srikrishnan, Thamarapu, Lijima, Herbert, Gesme, Jayson, Sapico, Leizl F., Paxton, Raymond, Grace, C. R., Nagenagowda, G., Lynn, A. M., Cowsik, Sudha M., Govil, G., Sahu, Sarata C., Bhattacharya, A., Chauhan, S., Kumar, Anil, Zuiderweg, Erik R. P., Pellecchia, Maurizio, Nitta, Katsutoshi, Ohnishi, Atsushi, Kawano, Keiichi, Hikichi, Kunio, Fujitani, Naoki, Ohkubo, Tadayasu, Aizawa, Tomoyasu, Kumaki, Yasuhiro, Hayakawa, Yoichi, Parvathy, Rani V., Kini, R. M., Nakagawa, Astushi, Tanaka, Isao, Demura, Makoto, Yao, Min, Koshiba, Takumi, Kobashigawa, Yoshihiro, Kuwajima, Kunihiro, Linge, Jens, Nilges, Michael, Donoghue, Seán O., Chakshusmathi, G., Ratnaparkhi, Girish S., Madhu, P. K., Varadarajan, R., Tetreau, C., Tourbez, M., Lavalette, D., Bulone, D., Manno, M., Emanuele, A., Palma-Vittorelli, M. B., Palma, M. U., Vaiana, S. M., Martorana, V., Biagio, P. L. San, Chang, D. K., Cheng, S. F., Yang, S. H., Francis, S., Trivedi, V. D., Chien, W. J., Manstein, Dietmar J., Batra, Renn, Geeves, Michael A., Geller, Maciej, Trvlska, Joanna, Grochowski, Pawel, Lesyng, B., Ginalski, K., Grochowski, P., Lavalette, P., Blouquit, Y., Roccatano, D., Berendsen, H. J. C., Amadei, A., Nola, Di A., Ho, Bosco, Curmi, P. M. G., Berry, H., Pelta, J., Pauthe, E., Lairez, D., Srinivasan, M., Sahi, Shakti, Kothekar, V., Madhusudnan, Kartha S., Nandel, Fateh S., Jain, D. V. S., Berendsen, Herman J. C., Feenstra, Anton K., Tama, F., Sanejouand, Y.-H., Go, N., Sharma, Deepak, Pasha, Santosh, Sharma, Sunita, Brahmachari, Samir K., Makker, Jyoti, Viiavaraghavan, R., Kumar, S., Dey, Sharmisllia, Krishnamoorthy, G., Lakshmikanth, G. S., Zaitseva, E. M., Mazhul, V. M., Kierdaszuk, Borys, Widengren, J., Rigler, R., Terry, B., Mets, Ü., Swaminathan, R., Yathindra, N., Thamotharan, S., Chosrowjan, H., Mataga, N., Shibata, Y., Morisima, I., Xiao, Ming, Selvin, Paul, Chakraharty, Tania, Cooke, Roger, Faraone, A., Branca, C., Maisano, G., Migliardo, P., Magazù, S., Villari, V., Behere, Digambar V., Deva, Sharique Zahida Waheed M., Vallone, B., Savino, C., Travaglini-Allocatelli, C., Cutruzzolà, F., Brunori, M., Gibson, Q. H., Mazumdar, Shyamalava, Mitra, Samaresh, Prasad, Swati, Soto, P., Fayad, R., Tyulkova, N. A., Sukovataya, I. E., Mamedov, Sh. V., Aksakal, B., Canturk, M., Aktas, B., Yilgin, R., Bogutska, K. I., Miroshnichenko, N. S., Wein, A. J., Hypolite, J. A., DiSanto, M., Chacko, S., Zheng, Y-M., Antosiewicz, J., Wojciechowski, M., Grycuk, T., Di Nola, Alfredo, Ceruso, Marc A., Chatterjee, Bishnu P., Bandvopadhvay, Subhasis, Choudhury, Devapriva, Khight, Stefan, Thompson, Andrew, Stojanoff, Vivian, Pinkner, Jerome, Hultgren, Scott, Flatters, Delphine, Goodfellow, Julia, Takazawatt, Fumi, Kanehisa, Minoru, Sasai, Masaki, Nakamura, Hironori, Wang, Bao Han, Pan, xin Min, Zheng, Yuan, Wang, Zhi Xin, Ahmad, Atta, Kulkarni, Sangeeta, Prakash, Koodathingal, Prajapati, Shashi, Surin, Alexey, Kihara, Hiroshi, Yang, Li, Matsumoto, Tomoharu, Nakagawa, Yuki, Semisotnov, Gennady V., Kimura, Kazumoto, Amemiya, Yoshiyuki, Tayyab, Saad, Muzammil, Salman, Kumar, Yogesh, Bhakuni, Vinod, Sundd, Monica, Kundu, Suman, Jagannadham, Medicherla V., Chandani, Bina, Warrier, Deepti, Sinha, Lalankumar, Dhar, Ruby, Mehrotra, Sonam, Khandelwal, Purnima, Seth, Subhendu, Gidwani, Arun, Prabha, Ratna C., Sasidhar, Y. U., Madhusudan, K. 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K., Sengupta, B., Sridevi, K., Kasturi, S. R., Gupta, S. P., Agarwal, Gunjan, Briehl, Robin W., Kwong, Suzanne, Tyulkova, N A., Ismailova, O. I., Parola, A. H., Yayon, A., Hariharan, C., Pines, D., Pines, E., Zamai, M., Cohen-Luria, R., Woolfeon, D. N., Spooner, G. A., Padya, M. J., Bharadwaj, D. K., Bakshi, Panchan, Jagannathan, N. R., Sharma, U., Srivastava, N., Barthwal, R., Matsuda, Keiko, Nishioka, Takaaki, Go, Nobuhiro, Urata, S., Aita, T., Husimi, Y., Majumder, Mainak, Subirana, Juan A., Malinina, Lucy, Abrescia, Nicola G. A., Aymami, Juan, Coll, Miquel, Eritxa, Ramón, Premraj, B. J., Thenmalarchelvi, R., Gautham, N., Kumar, Satheesh P., Kan, Lou-Sing, Hou, Ming, Lin, Shwu-Bin, Roy, Kanal B., Sana, Tapas, Bruant, N., Flatters, D., Lavery, R., Sklenar, Heinz, Rons, Remo, Lavery, Richard, Thakur, Ashoke Ranjan, Kundu, Sudip, Bandyopadhyay, Debashree, Bhattacharyya, Dhananjay, Majumdar, Rabi, Barceló, F., Portugal, J., Rao, B. J., Ramanathan, Sunita, Gliosli, Mahua, Varshney, Umesh, Kumar, Vinay N., Pataskar, Shashank S., Sarojini, R., Selvasekarapandian, S., Kolandaivel, P., Sukumar, S., Kolmdaivel, P., Maiti, Motilal, Das, Suman, Sen, Anjana, Xodo, Luigi, Suraci, Chiara, Del Terra, Elisa, Quadrifoglio, Franco, Diviacco, Silvia, Ray, Arghya, Rao, Basuthkar J., Karthikeyan, G., Chary, Kandala V. R., Mujeeb, Anwer, James, Thomas L., Bogdanov, A., Zanina, A., Haya, E. E. F., Kasyanenko, N., Cornélio, M. L., Bugs, M. R., Tolstorukov, Ye. M., Sanval, Nitish K., Tiwari, S. N., Sanyal, Nitish K., Choudhury, Mihir Roy, Patel, P. K., Bhavesh, Neel S., Gabrielian, Anna, Rigler, Rudolf, Edman, Lars, Wennmalm, Stefan, Constantinescu, B., Gazdaru, D., Radulcscu, I., Radu, L., Wärmländer, Sebastian, Aoki, Setsuyuki, Ishiura, Masahiro, Kondo, Takao, Pashinskaya, V. A., Kosevich, M. V., Shelkovsky, V. S., Blagoy, Yu. P., Wang, Ji-hua, Malathi, R., Chandrasekhar, K., Kandimalla, E. R., Agrawal, S., Rastogi, V. K., Palafox, Alcolea M., Singh, Chatar, Beniaminov, A. D., Minyat, E. E., Zdobnov, E. M., Ulyanov, N. B., Bondarenko, S. A., Ivanov, V. I., Singh, J. S., Tewari, Ravindra, Sonawane, Kailas D., Grosjean, Henri, Sonavane, Uddhavesh B., Morin, Annie, Doherty, Elizabeth A., Doudna, Jennifer A., Tochio, H., Shirakawa, M., Kyogoku, Y., Das, Achintya, Javaram, B., Kalra, Parul, Shukla, Piyush, Dixit, Surjit B., Beveridge, David L., McConnell, Kevin, Davidson, B. E., Chan, R. Y. S., Sawyer, W. H., Eccelston, J. F., Yan, Yuling, Norden, Bengt, Tuite, Eimer, Nielsen, Peter, Takahashi, Masayuki, Ghosh, Anirban, Bansal, Manju, Pingoud, Alfred, Christ, Frauke, Thole, Hubert, Pingoud, Vera, Wende, Wolfgang, Luthra, Pratibha Mehta, Chandra, Ramesh, Sen, Ranjan, Weisberg, Robert, King, Rodney, Gobets, Bas, van Amerongen, Herbert, van Stokkum, Ivo H. M., Larsen, Olaf F. A., van Grondelle, Rienk, Hilbers, Cornelis W., Heus, Hans A., Berends, Jos, Sngrvan, H E., Khudaverdian, N. V., Babayan, Yu. S., Pichierri, F., Gromiha, M., Prabakaran, P., Aida, M., Sayano, K., Merkienė, Eglė, Vilkaitis, Giedrius, Klimašauskas, Saulius, Serva, Saulius, Weinhold, Elmar, Bandiera, Antonella, Marsich, Eleonora, Manzini, Giorgio, Potikyan, G., Arakelyan, V., Babayan, Yu., Ninaber, Alex, Goodfellow, Julia M., Ohta, Shigeru, Ito, Yoichiro, Husimi, Yuzuru, Usukura, J., Aiba, H., Tagami, H., Nunes, Elia, Suarez, Mougli, Candreva, Carmen E., Keszenman, Deborah, Thyberg, Per, Földes-Papp, Zeno, Joshi, Amita, Singh, Dinesh, Rajeswari, M. R., Amenitsch, H., Pregetter, M., Chapman, J., Mishra, K. P., Pandev, B. N., Tonevitsky, A. G., Pohl, E. E., Agapov, I. I., Sun, J., Pohl, P., Dennison, S. M., Gorbeako, G. P., Dynbko, T. S., Mishra, A. K., Pappavee, N., Luis, Loura, Rodrigo, Almeida, Manuel, Prieto, Gendel, Ya. L., Kleszczyńska, H., Kuczera, J., Przestalski, S., Kral, T., Chernitsky, E. A., Senkovich, O. A., Rosin, V. V., Gasanov, R. A., Allakhverdieva, Y. M., Papageorgiou, G. C., Savopol, Tudor, Apetrei, Calin, Balea, Marius, Cucu, D., Mihailescu, D., Ramanathan, K. V., Bačić, Goran, Genest, Monique, Sajot, Nicolas, Garnier, Norbert, Crouzy, Serge, Zsiros, O., Várkonyi, Z. S., Combos, Z., Farkas, T., Cribier, Sophie, de Paula, F., Fraceto, I. F., Schreier, S., Spisni, A., Sevšek, F., Žekš, B., Gomišček, G., Svetina, S., Arrigler, V., Hotani, Hirokazu, Nomura, Fumimasa, Takiguchi, Kingo, Nagata, Miki, Panicker, Lata, Parvathanathan, P. S., Hotani, H., Takiguchi, K., Ishino, A., Saitoh, A., Afonin, S., Takahashi, A., Takizawa, T., Nakato, Y., Marathe, Dipti, Jørgensen, Kent, Chattopadhyay, Amitabha, Rukmini, R., Rawat, Satinder S., Pečar, S., Štrancar, J., Šentiurc, M., Stolič, Z., Filipin, K., Biswas, S. C., Samanta, Anunay, Sana, Satyen, Kinoshita, Koji, Yamazaki, Masahito, Ohki, Kazuo, Goto, Akira, Kiuchi, Tai, Kumeta, Takaaki, Ohba, Tetsuhiko, Sugar, I. P., Thompson, K. K., Biltonen, R. L., Thompson, T. 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R., Hicks, D., Dreyfus, H., Sahel, J., Picaud, S., Forster, V., Wang, Hong-Wei, Sui, Sen-fang, Luther, Pradeep K., Morris, Ed, Barry, John, Squire, John, Sundari, Sivakama C., Balasubramanian, D., Christlet, Hema Thanka T., Veluraia, K., Suresh, Xavier M., Laretta-Garde, V., Krilov, Dubravka, Herak, Janko N., Stojanović, Nataša, Ferrone, Frank A., Ivanova, Maria, Jasuja, Ravi, Mirchev, Rossen, Stopar, David, Wolfs, Cor J. A. M., Hemminga, Marcus A., Spruijt, Ruud B., Arcovito, G., De Spirito, M., Frank, Joachim, Heagle, Amy B., Grassucci, Robert, Penczek, Pawel, Agrawal, Rajendra K., Sharma, Manjuli R., Wagenknecht, Terence, Jeyakumar, Loice H., Fleischer, Sidney, Knupp, Carlo, Squire, John M., Ezra, Eric, Munro, Peter M. G., Kitazawa, Hidefumi, Ichihara, Koji, Itoh, Tomohiko J., Iguchi, Yusuke, Pifat, Greta, Kveder, Marina, Pečar, Slavko, Schara, Milan, Nair, Deepak, Singh, Kavita, Rao, Kanury V. S., Sundaravadivel, B., Jain, Deepti, Kaur, Kanwaljeet, Salunke, D. M., Goel, Manisha, Kovalenko, E. I., Semenkova, G. N., Cherenkevich, S. N., Loganathan, D., Lakshmanan, T., Sriram, D., Srinivasan, S., Lebrón, J. A., Bjorkman, P. J., Ramalingam, T. S., Singh, A. K., Gayatri, T. N., Bisch, Paulo M., Caffarena, Ernesto R., Grigera, Raul J., Fromherz, P., Kiessling, V., Suresh, C. G., Rao, K. N., Khan, M. I., Gaikwad, S. M., Elanthiraiyan, M., Kaliannan, P., Payne, J., Chadha, K., Ambrus, J. L., Nair, M. P. N., Nair, Madhavan P. N., Hewitt, R., Schwartz, S. A., Mahajan, S., Macherel, D., Bourguignon, J., Neuburger, M., Douce, R., Cohen-Addad, C., Faure, M., Ober, R., Sieker, L., Gurumurthy, D. S., Velmurugan, S., Lobo, Z., Phadke, Ratna S., Desai, Prashant, Alieva, D. R., Guseinova, I. M., Zulfugarov, I. S., Aliev, J. A., Ismayilov, M. A., Novruzova, S. N., Savchenko, T. V., Suleimanov, Yu. S., Bartošková, Hana, Nauš, Jan, Ilík, Petr, Kouřil, Roman, Vidyasagar, P. B., Thomas, Sarah, Gaikwad, Jvoti U., Cseh, Z., Mustárdy, L., Garab, G., Simidjiev, I., Rajagopal, S., Várkonyi, Zs., Holzenburg, A., Stoylova, S., Papp, E., Millar, D. P., Bruder, R., Woo, T. T., Genick, U. K., Gerwert, K., Jávorfí, Tamás, Garab, Győző, Naqvi, Razi K., Gaikwad, Jyoti, Kalimullah, Md., Semwal, Manoj, Naus, Man, Ilik, Petr, Kouril, Roman, Horváth, Gábor, Bernard, Gary D., Pomozi, István, Wehner, Rüdiger, Damjanović, Ana, Schulten, Klaus, Ritz, Thorsten, Yandao, Gong, Jushuo, Wang, Nanming, Zhao, Jixiu, Shan, Freiberg, Arvi, Timpmann, Kõu, Woodbury, Neal W., Ruus, Rein, Nemtseva, E. V., Kudryasheva, N. S., Sizykh, A. G., Tikhomirov, A. A., Nesterenko, T. V., Shikhov, V. N., Forti, Giorgio, Furia, Alberto, Finazzi, Giovanni, Barbagallo, Romina Paola, Agalarov, R., Gasanov, R., Iskenderova, S., Nobuhiro, G. O., Osamu, Miyashita, Ramrakhiani, M., Soni, R. K., Yoshida, Masasuke, Akutsu, Hideo, Yagi, Hiromasa, Tozawa, Kacko, Sekino, Nobuaki, Iwabuchi, Tomoyuki, Kaulen, A. D., Avetisyan, A. V., Feniouk, B. A., Skulachev, V. P., Breyton, Cécile, Kühlbrandt, Werner, Gräslund, Astrid, Assarsson, Maria, Libisch, B., Horváth, G., Gombos, Z., Budagovskaya, N. V., Kudryasheva, N., Fukunishi, Arima, Harada, Erisa, Fukuoka, Yuki, Ohmura, Tomoaki, Kawai, Gota, Watanabe, Kimitsuna, Žekš, Boštjan, Božič, Bojan, Derganc, Jure, Svetina, Saša, Hoh, J. F. Y., Li, Z. B., Rossmanith, G. H., Frederix, P. L. T. M., de Beer, E. L., Treijtel, B. W., Blangè, T., Galtet, F., Hénon, S., Isabey, D., Planus, E., Laurent, V., Rath, L. S., Raval, M. K., Dash, P. K., Ramakrishnan, C., Balaram, R., Basak, Kanika, Balaban, Alexandra T., Nandy, Ashesh, Grunwald, Gregory D., Vracko, Marjan, Randic, Milan, Basak, Subhash C., Amic, Dragan, Beslo, Drago, Trinajstic, Nenad, Nikolic, Sonja, Walahaw, J., Lensink, Marc F. J., Reddy, Boojala V. B., Shindylov, Ilya N., Bourne, Philip E., Grigera, J. R., de Xammar Oro, J., Donnamaria, M. C., Neagu, Monica, Neagu, Adrian, Janežič, Dušanka, Praprotnik, Matej, Nilsson, Lennart, Mark, Pekka, Fata, La L., Dardenne, Laurent E., Werneck, Araken S., Neto, Marçal de O., Kannan, N., Vishveshwara, S., Veluraja, K., Opitz, David, Balasubramanian, Krishnan, Gute, Brian D., Mills, Denise, Lungeanu, Diana, Mihalas, G. I., Macovievici, G., Gruia, Raluca, Dalcin, B., Cortez-Maghelly, C., Passos, E. P., Ljubisavljevic, M., Blesic, S., Milosevic, S., Stratimirovic, D. J., Bachhawat, Nandita, Mande, Shekhar C., Nandy, A., Nishigaki, Koichi, Saito, Ayumu, Naimuddin, Mohammed, Takaesu, Hirotomo, Ono, Mitsuo, Hirokawa, Takatsugu, Eissa, A. M., Ahmed, Abdalla S., El Gohary, M. I., Nakashima, Hiroshi, Raghava, G. P. S., Kurgalvuk, N., Goryn, O., Gerstman, Bernard S., Kratasyuk, V. A., Esimbekova, E. N., Gritsenko, E. V., Remmel, N. N., Maznyak, O. M., German, A., Tikhonov, A., Tchitchkan, D., Koulchitsky, S., Pashkevich, S., Pletnev, S., Kulchitsky, V., Pesotskaya, Y., Shapiro, Erik M., Borthakur, Arijitt, Dimitrov, Ivan, Leigh, John S., Rizi, Rahim, Reddy, Ravinder, Charagundla, Sridhar, Duvvuri, Umamaheswar, Degaonkar, M., Khubchandani, M., Kumar, Mahesh, Jagannathan, N R., Raghunathan, P., Jayasundar, Rama, Coshic, O., Rath, O. K., Julka, P. K., Iliescu, Karina Roxana, Sajin, Maria, Petcu, Ileana, Moisoi, Nicolcta, Kuzmenko, A. I., Donchenko, G. V., Nikolenko, I. A., Morozova, R. P., Rahman, M. K., Ahmed, M. M., Watanabe, Takehiro, Uretzky, G., Ammar, R., Sharony, R., Rubin, Y., Gilboa, H., Mallick, H. N., Kumar, Mohan V., Begum, Gulnaz M., Degaonkar, Mahaveer N., Govindasamy, S., Kumosani, T. A., Lupusoru, C., Titescu, G., Haulica, I., Stefanescu, I., Iliescu, R., Nastasa, V., Bild, W., Khetawat, Gopal, Nealen, M., Faraday, N., Bray, P. F., Noga, S., Lycholat, E. A., Ananieva, T. V., Kosevich, M V., Stepanyan, S. G., Antonyuk, S. V., Khachatryan, A., Kumar, A., Arakelian, H., Khachatryan, R., Agadjanyan, S., Ayrapetyan, S., Mkheyan, V., Rajan, S. S., Kabaleeswaran, V., Gopalakrishnan, Geetha, Govindachari, T. R., Ramrakhiani, Meera, Cullen, David C., Lowe, Phillip, Badley, Andrew, Hermel, H., Möhwald, H., Schmahl, W., Singh, Anil K., Das, Joydip, Majumdar, Nirmalya, Dér, András, Oroszi, László, Kelemen, Loránd, Ormos, Pál, Hámori, András, Ramsden, Jeremy J., Mitra, Chanchal K., Savitri, D., Yanagida, Toshio, Esaki, Seiji, Sowa, Yosiyuki, Nishida, Tomoyuki, Kimura, Yuji, Radu, M., Laukhina, E. E., Kasumova, L. A., Koltover, V. K., Bubnov, V. P., Estrin, Ya. I., Dotta, Rajiv, Zahradník, Ivan, Marko, Milan, Novák, Pavel, Miyata, Hidetake, Hirata, Hiroaki, Sengupta, P., Maiti, S., Balaji, J., Banerjee, S., Barker, A. L., Winlove, C. P., OʼHare, D., Macpherson, J. V., Gonsalves, M., Unwin, P. R., Phillip, R., Kumar, Ravindra G., Murata, K., Nagayaka, K., Danev, R., Sugitani, S., Gősch, Michael, Thyberg, P., Földes-Papp, Z., Björk, G., Blom, H., Holm, J., Heino, T., Inagaki, Fuyuhiko, Yokochi, Masashi, Kusunoki, Masami, Matthews, E. K., Pines, J., Chukova, Yu. P., Koltover, Vitaly K., Kang, B. P. S., Bansal, Geetanjali, Bansal, M. P., Singh, U., Singh, Uma, Nakata, Kotoko, Nakano, Tastuya, Kaminuma, Tsuguchika, Kirn, Bonn, Potocnik, Neja, Stare, Vito, Shukla, Latal, Sastry, M. D., Natarajan, V., Devasagayam, T. P. A., Kesavan, P. C., Sayfutdinov, R., Degermendzhy, A. G., Adamovich, V. V., Rogozin, Yu. D., Khetrapal, C. L., Gowda, G. A. Nagana, Ghimire, Kedar Nath, Masaru, Ishida, Fujita, H., Ishiwata, S., Suzuki, M., Kawahara, S., Kirino, Y., Kishimoto, Y., Mori, H., Mishina, M., Ohshima, H., Dukhin, A. S., Goetz, P. J., Shilov, V. N., and Mishra, R. K.

Published
1999
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10. Radiation Engineering of Xyloglucan Hydrogels

Author

TODARO, Simona, SABATINO, Maria Antonietta, Ajovalasit, Alessia, Ditta, Lorena Anna, DISPENZA, Clelia, Castiglia, D., Wach, R., Ulanski, P., Bulone, D., Todaro, S., Sabatino, M., Ajovalasit, A., Ditta, L., Castiglia, D., Wach, R., Ulanski, P., Bulone, D., and Dispenza, C.

Subjects
lcsh:Computer engineering. Computer hardware, lcsh:TP155-156, Chemical Engineering (all), lcsh:TK7885-7895, lcsh:Chemical engineering
Abstract

Xyloglucans (XGs) are interesting substrates for the production of scaffolds for tissue engineering, drug delivery depots and hydrogel dressings, thanks to their ability to gel in appropriate conditions, such as in the presence of hydro-alcoholic solvents or by addition of sugar molecules. Due to their natural source, they are characterized by high average molecular weights and broad molecular weight distributions. High energy irradiation is a suitable tool to reduce polysaccharides molecular weight without a dramatic alteration of the polymer chemical structure and gelation ability. In this work, the effect of the radiation dose on the molecular weight of a XG derived from Tamarind seeds is investigated. The rheological properties of the gels obtained by adding ethanol to the polymer water solutions are also described. The effects of alcohol content, storage time and irradiation dose on gel strength are discussed.

Published
2016

11. Studies of network organization and dynamics of e-beam crosslinked PVPs: From macro to nano

Author

Dispenza, C., Grimaldi, N., Sabatino, M., Bulone, D., Todaro, S., Giacomazza, D., Przybytniak, G., Alessi, S., Spadaro, G., Dispenza, C, Grimaldi, N, Sabatino, MA, Bulone, D, Todaro, S, Giacomazza, D, Przybytniak, G, Alessi, S, and Spadaro, G

Subjects
chemistry.chemical_classification, Radiation, Materials science, Aqueous solution, NMR spin–lattice relaxation, Spin–lattice relaxation, Nanogels, Polymer, Dynamic mechanical analysis, e-Beam irradiation, PVP aqueous solutions, Dynamic mechanical spectroscopy, Nanogel, Polymerization, Chemical engineering, chemistry, Nano, Polymer chemistry, Electron beam processing, PVP aqueous solution, Settore CHIM/07 - Fondamenti Chimici Delle Tecnologie, NMR spin-lattice relaxation
Abstract

In this work the influence of poly(N-vinyl pyrrolidone) (PVP) concentration in water on the organization and dynamics of the corresponding macro-/nanogel networks has been systematically investigated. Irradiation has been performed at the same irradiation dose (within the sterilization dose range) and dose rate. In the selected irradiation conditions, the transition between macroscopic gelation and micro-/nanogels formation is observed just below the critical overlap concentration (∼1 wt%), whereas the net prevalence of intra-molecular over inter-molecular crosslinking occurs at a lower polymer concentration (below 0.25 wt%). Dynamic–mechanical spectroscopy has been applied as a classical methodology to estimate the network mesh size for macrogels in their swollen state, while 13C NMR spin–lattice relaxation spectroscopy has been applied on both the macrogel and nanogel freeze dried residues to withdraw interesting information of the network spatial organization in the passage of scale from macro to nano.

Published
2012

12. Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

Author

Spigolon, D., Gallagher, D.T., Velázquez-Campoy, Adrián, Bulone, D., Narang, J., San Biagio, P.L., Cappello, F., Macario, A.J.L., Conway de Macario, E., Robb, F.T., Spigolon, D., Gallagher, D.T., Velázquez-Campoy, Adrián, Bulone, D., Narang, J., San Biagio, P.L., Cappello, F., Macario, A.J.L., Conway de Macario, E., and Robb, F.T.

Abstract

The human chaperonin complex is a ~ 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy in humans. In previous work, we introduced an equivalent mutation in an archaeal chaperonin that assembles into two octameric rings like in humans but in which all subunits are identical. We reported that the hexadecamer formed by the mutant subunit is unstable with impaired chaperoning functions. This study quantifies the loss of structural stability in the hexadecamer due to the pathogenic mutation, using differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC). The disassembly of the wild type complex, which is tightly coupled with subunit denaturation, was decoupled by the mutation without affecting the stability of individual subunits. Our results verify the effectiveness of the homo-hexadecameric archaeal chaperonin as a proxy to assess the impact of subtle defects in heterologous systems with mutations in a single subunit.

Published
2017

13. POLYSACCHARIDE-BASED HYDROGELS FOR MYOCARDIUM REMODELING

Author

Pasta, S, Scardulla, Francesco, Bulone, D, Scardulla, C., TODARO, Simona, SABATINO, Maria Antonietta, Ajovalasit, Alessia, RINAUDO, Antonino, SPADARO, Giuseppe, DISPENZA, Clelia, Pasta, S, Todaro, S, Sabatino, MA, Ajovalasit, A, Scardulla, F, Rinaudo, A, Spadaro, G, Bulone, D, Dispenza, C, and Scardulla, C

Subjects
Hydrogels, Settore CHIM/07 - Fondamenti Chimici Delle Tecnologie
Published
2014

16. Effect of HSP60 on fibrillogenesis of A-beta amyloid peptide

Author

Mangione, M., Marino, C., Vilasi, S., Spigolon, D., Passantino, R., Canale, C., Bulone, D., San Biagio, P., CAPPELLO, Francesco, Mangione, M., Marino, C., Vilasi, S., Spigolon, D., Passantino, R., Canale, C., Cappello, F., Bulone, D., and San Biagio, P.

Subjects
Alzheimer Hsp60 Aggregation
Abstract

Alzheimer Hsp60 Aggregation

Published
2014

19. Radiation engineering of xyloglucan hydrogels

Author

Todaro S., Sabatino M.A., Ajovalasit A., Ditta L.A., Castiglia D., Wach R.A., Ulanski P., Bulone D., and Dispenza C.

Subjects
Hydrogel, physical gelation, scaffold, Xyloglucan
Abstract

Xyloglucans (XGs) are interesting substrates for the production of scaffolds for tissue engineering, drug delivery depots and hydrogel dressings, thanks to their ability to gel in appropriate conditions, such as in the presence of hydro-alcoholic solvents or by addition of sugar molecules. Due to their natural source, they are characterized by high average molecular weights and broad molecular weight distributions. High energy irradiation is a suitable tool to reduce polysaccharides molecular weight without a dramatic alteration of the polymer chemical structure and gelation ability. In this work, the effect of the radiation dose on the molecular weight of a XG derived from Tamarind seeds is investigated. The rheological properties of the gels obtained by adding ethanol to the polymer water solutions are also described. The effects of alcohol content, storage time and irradiation dose on gel strength are discussed

Published
2016

24. Naïve Hsp60, similarly to GroEL, oligomerizes to build heptameric and tetradecameric structures

Author

MARINO GAMMAZZA, Antonella, CAMPANELLA, Claudia, BURGIO, Giosalba, ZUMMO, Giovanni, CAPPELLO, Francesco, Vilasi, S, Carrotta, R, Mangione,MR, Librizzi, F, Martorana,V, Ortore,MG, Vilasi,A, Corona,D, Bulone,D, Conway de Macario,E, Macario, AJL, San Biagio, PL, Marino Gammazza,A, Vilasi, S, Carrotta, R, Mangione,MR, Campanella,C, Librizzi, F, Martorana,V, Ortore,MG, Vilasi,A, Burgio, G, Corona,D, Zummo,G, Bulone,D, Conway de Macario,E, Macario, AJL, San Biagio, PL, and Cappello F

Subjects
Hsp60, structure, Groel
Published
2013

25. Density, structural lifetime, and entropy of H-bond cages promoted by monohydric alcohols in normal and supercooled water.

Author

Bulone, D., Donato, I. D., Palma-Vittorelli, M. B., and Palma, M. U.

Subjects
*THERMODYNAMICS, *ENTROPY
Abstract

Density data for aqueous solutions of monohydric alcohols down to supercooling are presented and combined with data concerning viscosity of the same systems, and with available data on pure water. Two conceptually different families of longer-lived, high-connectivity H-bond structures can be sorted out in the irregular, frequently restructured network of H bonds: spontaneous structures, as in pure water, and alcohol-induced structures. Molar volumes for both are obtained and compared, allowing microscopic conclusions which agree quantitatively with available thermodynamic data. For the three alcohols studied, the well-known negative excess entropy of mixing shows a strict proportionality to the fraction of water molecules sorted out in our study as taking statistically part in alcohol-promoted cages. The remarkable proportionality extends to all alcohols, all concentrations, and all temperatures studied. Apparent (and expected) geometric distortions of alcohol-promoted cages do not affect this proportionality. However, they can be related to disturbing effects on the singular behavior of several properties of cold and supercooled water. These results are further combined with the only available quantitative data on the modulation by alcohols of the hydrophobic contribution to the functional conformational switching of a biomolecule. This allows for the first time deriving, from experiments on a protein solution, the statistical number of water molecules and associate entropy change directly involved in a specific protein function (oxygen uptake/release by human hemoglobin HbA in the specific case). Compared to the bare protein, this functional unit is largely stabilized as a consequence of the remarkably higher dimensionality in its phase space. [ABSTRACT FROM AUTHOR]

Published
1991
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26. Viscosity of aqueous solutions of monohydric alcohols in the normal and supercooled states.

Author

Bulone, D., Spinnato, C., Madonia, F., and Palma, M. U.

Subjects
*TEMPERATURE, *LIGHT scattering, *LOW temperatures
Abstract

Viscosities of solutions of Met-, Et-, and n-PropOH were measured by quasielastic light scattering of polystyrene lattice spheres of 800 Å diameter, in the low-concentration, low-temperature ranges where effects of alcohols on the structure and properties of liquid water are most pronounced. Raw data already indicate that alcohols promote the formation of clathrate-like structures of H bonds which add to those occurring naturally in the pure solvent. Evaluation of the number of water molecules taking part in longer-lived structures further indicates that this promotion is most effective in the infinite-dilution limit. Available thermodynamic data agree with this evaluation. Mismatches among solute-promoted clathrate-like cages are evidenced. The known disruptive effects of alcohols on the anomalous properties of cold and supercooled water are thus understood in terms of limitations to the correlation length of density fluctuations, set by mismatches. A contribution of OH groups to cage promotion is also evidenced at least at low temperature. Constraints or hindrances to the motion of water molecules, irrespective of their nature, appear to be effective in favoring structures of stabler, longer-lived H bonds, corresponding to water molecules of lower mobility. This offers a unified view of hydrophobic and hydrophilic interactions which agrees with earlier work and with more recent computer experiments. The possibility here evidenced for structures of H bonds promoted in solvent water of being conflictual or synergistic, adds to the microscopic understanding of solvent-mediated interactions, e.g., of biosolutes. [ABSTRACT FROM AUTHOR]

Published
1989
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27. Radiation sculpured nanogels as platform for novel therapeutic systems

Author

Clelia Dispenza, Sabatino, Maria Antonietta, Grimaldi, Natascia, Alessi, Sabina, Spadaro, Giuseppe, Bulone, D., Bondì, M., Casaletto, M., Adamo, G., Salvatrice Rigogliuso, Giulio Ghersi, Dispenza, C, Sabatino, MA, Grimaldi, N, Alessi, S, Spadaro, G, Bulone, D, Bondì, ML, Casaletto, MP, Adamo, G, Rigogliuso, S, and Ghersi, G

Subjects
nanomedicine, radiation chemistry, nanogels, Settore CHIM/07 - Fondamenti Chimici Delle Tecnologie
Published
2012

28. Large-scale Radiation Manufacturing of Hierarchically Assembled Nanogels

Author

DISPENZA, Clelia, SABATINO, Maria Antonietta, GRIMALDI, Natascia, SPADARO, Giuseppe, ADAMO, Giorgia, RIGOGLIUSO, Salvatrice, Bulone, D, Bondì, ML, Bardone, E, Brucato, A, Keshavarz, T, Dispenza, C, Sabatino, MA, Grimaldi, N, Spadaro, G, Bulone, D, Bondì, ML, Adamo, G, and Rigogliuso, S

Subjects
Nanogels, Settore CHIM/07 - Fondamenti Chimici Delle Tecnologie
Abstract

Nanogels (NGs), or small particles formed by physically or chemically crosslinked polymer networks, represent a niche in the development of “smart” nanoparticles for drug delivery and diagnostics. They offer unique advantages over other systems, including a large and flexible surface for multivalent bio-conjugation; an internal 3D aqueous environment for incorporation and protection of (bio)molecular drugs; the possibility to entrap active metal or mineral cores for imaging or phototherapeutic purposes; stimuli-responsiveness to achieve temporal and/or site control of the release function and biocompatibility. The availability of inexpensive and robust preparation methodologies is at the basis of the development of effective nanogel-based theragnostic devices. The design rules for mass fabrication of nanoscale hydrogel particles with the recourse to industrial-type accelerators is here discussed.

Published
2012

29. Influence of exogenous and endogenous ions on the properties of BSA

Author

Giacomazza, G, Mangione, MR, Bulone, D, Martorana, V, San Biagio, PL, NAVARRA, Giovanna, Alekseev, RJ, Rebane, AL, Giacomazza, G, Mangione, MR, Bulone, D, Martorana, V, Navarra, G, and San Biagio, PL

Subjects
conformational change, Bovin serum albumin, aggregation, metal ion, Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin)
Published
2012

32. Entrapment of Aβ(1-40) peptide in unstructured aggregates

Author

Corsale, C, Carrotta, R, Mangione, MR, Vilasi, S, Provengano, A, Bulone, D, San Biagio, PL, CAVALLARO, Gennara, Corsale, C, Carrotta, R, Mangione, MR, Vilasi, S, Provengano, A, Cavallaro, G, Bulone, D, and San Biagio, PL

Subjects
fibrillogenesis
Abstract

Recognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that Aβ-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid β-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggregates. They appear stable or at least metastable with respect to fiber growth, therefore appearing as an incidental product in the pathway of fibrillogenesis

Published
2012

33. Radiation engineered functionalized nanogels as platform for biomedical nanocarriers

Author

Clelia Dispenza, Sabatino, Maria Antonietta, Bulone, D., Grimaldi, Natascia, Spadaro, Giuseppe, Bondì, M., Salvatrice Rigogliuso, Giulio Ghersi, Dispenza, C, Sabatino, MA, Bulone, D, Grimaldi, N, Spadaro, G, Bondì, ML, Rigogliuso, S, and Ghersi, G

Subjects
nanogels, Settore CHIM/07 - Fondamenti Chimici Delle Tecnologie
Published
2011

34. Studies of network structure and dynamics of e-beam crosslinked PVPs: From macro to nano

Author

DISPENZA, Clelia, GRIMALDI, Natascia, SABATINO, Maria Antonietta, TODARO, Simona, ALESSI, Sabina, SPADARO, Giuseppe, Bulone, D, Giacomazza, D, Przybytniak, G, Dispenza, C, Grimaldi, N, Sabatino, MA, Bulone, D, Giacomazza, D, Przybytniak, G, Todaro, S, Alessi, S, and Spadaro, G

Subjects
e-Beam irradiation,PVP aqueous solutions, Nanogels, Dynamic mechanical spectroscopy, NMR spin–lattice relaxation
Abstract

Much interest has been paid to develop a variety of radiation-crosslinked hydrated polymeric materials, which swell in water but do not dissolve, as biocompatible materials used for wound healing, drug delivery system, surface-coating material for medically used devices, etc. With the aim of establishing design rules to produce hydrogels of controlled size at the nanoscale and desired internal network structure using conventional electron accelerators and set-ups, here we attempt a description in terms of structural and dynamic properties of polymer networks generated through e-beam irradiation of aqueous solutions of the same model polymer, a commercial grade poly(N-vinyl-pyrrolidone), subjected to e-beam irradiation with a 12 MeV Linac accelerator, at same dose (40kGy) and dose-rate (100 kGy/h) and at the variance of polymer concentration in water. Concentration has been systematically varied from above (10, 8, 6, 4, 2 % w) to below (1, 0.5, 0.25, 0.1, 0.05 % w) the critical chain overlap concentration value (~1%w) of the chosen polymer in water, as estimated by intrinsic viscosity measurements. The transition between macroscopic gelation and micro-/nanogels formation is observed just below the critical overlap concentration (0.5 %w), whereas the net prevalence of intra-molecular over inter-molecular crosslinking occurs at a polymer concentration below 0.25 % w, as revealed by both dynamic and static laser light scattering measurements. Significant structural differences between nanoscalar “finite” crosslinked networks and macrogels are evidenced by both FTIR and solid state NMR spectra. Polymeric segments mobility of the formed networks, at the different scales, has been assessed through stress-rheometry, solid-state cross-polarization times and nuclear relaxation time NMR studies of the freeze-dried residues.

Published
2011

35. Macromolecular engineering of hydrogels: from macro to nano scalar materials for different levels of biointeraction

Author

Clelia Dispenza, Sabatino, Maria Antonietta, Bulone, D., Giacomazza, D., Giulio Ghersi, Maurizio Leone, Salvatrice Rigogliuso, Spadaro, Giuseppe, Dispenza, C, Sabatino, MA, Bulone, D, Giacomazza, D, Ghersi, G, Leone, M, Rigogliuso, S, and Spadaro, G

Subjects
Hydrogel, tissue engineering, drug delivery, bionanotechnology, Settore CHIM/07 - Fondamenti Chimici Delle Tecnologie
Published
2009

36. Oligomerizing ability of newly made human Hsp60 with its mitochondrial import signal

Author

Vilasi, S., Carrotta, R., Mangione, M.R., Campanella, C., Palumbo Piccionello, A., Librizzi, F., Martorana, V., Ortore, M.G., Marino Gammazza, A., Vilasi, A., Burgio, G., Corona, D., Zummo, G., Bulone, D., Conway De Macario, E., Macario, A.J.L., San Biagio, P.L., and Cappello, F.

Subjects
animal structures, fungi, chemical and pharmacologic phenomena, complex mixtures
Abstract

It is currently accepted that the human Hsp60 resides and works not only in the mitochondria, the canonical residence, but also outside it. It is also known that Hsp60 although coded by a nuclear gene is synthesized in the cytosol and includes an N-terminal mitochondrial import signal (MIS), which directs the polypeptide toward the inside of the organelle where the MIS is removed. Therefore, there are at least two functional types of Hsp60, with and without MIS, the former in the cytosol the latter inside the mitochondria. A key question is: how do these two forms of Hsp60 differ beyond the fact that while one has MIS the other lacks it? How presence or absence of MIS affects the ability of Hsp60 to form oligomers, which are considered important for chaperoning peptides and assist them to reach a native state? We report here our initial observations on this issue. Typically, in the mitochondria, Hsp60 forms ring-shaped heptamers, two of which associate to build a barrel-shaped tetradecamer, the functional chaperoning complex. It is not known if the cytosolic Hsp60 with its MIS, also forms hepta- and tetradecamers. A clarification of this issue will most likely shed light on the physiological functions of extramitochondrial Hsp60, and also on its pathogenic role in Hsp60 chaperonopathies. Consequently, we compared recombinant Hsp60 bearing the MIS with the prokaryotic ortholog GroEL, which under normal conditions forms functional double-ring tetradecamers. Characteristic hydrodynamic sizes of the oligomeric complex for both systems were investigated by small angle X-ray (SAXS) and static and dynamic light scattering (SLS and DLS) in solution under similar physicochemical conditions. High Performance Liquid Chromatography (HPLC) and blue native polyacrylamide-gel electrophoresis were used to further clarify the equilibrium between the different oligomeric species of the two proteins over a wide range of concentrations. Hsp60 with MIS formed hepta- and tetradecamers similarly to GroEL. Oligomerization was dependent on concentration for GroEL and Hsp60, but for the latter, formation of larger oligomers, e.g., tetradecamers, required higher concentrations than the former., Italian Journal of Anatomy and Embryology, Vol 118, No 2 (Supplement) 2013

Published
2014
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37. Kinetics of different processes in human insulin amyloid formation

Author

Manno M., Craparo E.F., Podestà A., Bulone D., Carrotta R., Martorana V., Milani P., Tiana G., San Biagio P.L., MANNO M, CRAPARO EF, PODESTA' A, BULONE D, CARROTTA R, MARTORANA V, TIANA G, and SAN BIAGIO PL

Subjects
Amyloid, medicine.medical_treatment, Kinetics, Microscopy, Atomic Force, Fibril, Models, Biological, Fluorescence, chemistry.chemical_compound, light-scattering, Structural Biology, amyloid fibril, Microscopy, medicine, Humans, Insulin, Scattering, Radiation, Microscopy, Phase-Contrast, Benzothiazoles, Particle Size, Molecular Biology, Fluorescent Dyes, atomic force microscopy, aggregation, Temperature, Hydrogen-Ion Concentration, Thiazoles, Crystallography, Monomer, chemistry, Biophysics, Thioflavin, Elongation
Abstract

Human insulin has long been known to form amyloid fibrils under given conditions. The molecular basis of insulin aggregation is relevant for modeling the amyloidogenesis process, which is involved in many pathologies, as well as for improving delivery systems, used for diabetes treatments. Insulin aggregation displays a wide variety of morphologies, from small oligomeric filaments to huge floccules, and therefore different specific processes are likely to be intertwined in the overall aggregation. In the present work, we studied the aggregation kinetics of human insulin at low pH and different temperatures and concentrations. The structure and the morphogenesis of aggregates on a wide range of length scales (from monomeric proteins to elongated fibrils and larger aggregates networks) have been monitored by using different experimental techniques: time-lapse atomic force microscopy (AFM), quasi-elastic light-scattering (QLS), small and large angle static light-scattering, thioflavin T fluorescence, and optical microscopy. Our experiments, along with the analysis of scattered intensity distribution, show that fibrillar aggregates grow following a thermally activated heterogeneous coagulation mechanism, which includes both tip-to-tip elongation and lateral thickening. Also, the association of fibrils into bundles and larger clusters (up to tens of microns) occurs simultaneously and is responsible for an effective lag-time.

Published
2007

43. Structure of e-beam sculptured poly(N-vinylpyrrolidone) networks across different length-scales, from macro to nano

Author

Sabatino MA, Bulone D, Veres M, Spinella A, Spadaro G, and Dispenza C

Subjects
Nanogels, Poly(N-vinylpyrrolidone), Irradiation
Abstract

Study of macromolecular structure and dynamics of networks formed by pulsed electron-beam irradiation of poly(N-vinyl pyrrolidone) (PVP) aqueous solutions, at relatively low energy per pulse and across different concentration regimes, provides the basis for the understanding of a new generation of functional nanostructures. Networks are the result of the follow-up reactions initiated by a continuous series of electron pulse-generated hydroxyl radicals, which may have a different fate at the variance of polymer concentration. Different spectroscopic techniques, FT-IR, 13C {1H} CP-MAS NMR and Raman, applied to characterize the formed networks, describe a profound modification of the chemical structure when network size is approaching the nanoscale. Static light scattering measurements provide further information on the average weight molecular weight modification of PVP when forming nanogel particles. From the simultaneous control of network size and modification of chemical functionality stems also an intrinsic fluorescence of these nanogels never observed before. Altogether the obtained radiation-sculptured nanogels exhibit interesting multifunctionality that, coupled with the already proven biocompatibility, can be exploited in the biomedical field.

Published
2013

45. Inhibiting effect of alpha(s1)-casein on A beta(1-40) fibrillogenesis

Author

Carrotta R, Canale C, Diaspro A, Trapani A, San Biagio PL, and Bulone D

Subjects
ALPHA-B-CRYSTALLIN, SMALL-MOLECULE INHIBITORS, AMYLOID-BETA-PROTEIN, ATOMIC-FORCE MICROSCOPY
Abstract

Background: alpha(s1)-Casein is one of the four types of caseins, the largest protein component of bovine milk. The lack of a compact folded conformation and the capability to form micelles suggest a relationship of alpha(s1)-casein with the class of the intrinsically disordered (or natively unfolded) proteins. These proteins are known to exert a stabilizing activity on biomolecules through specific interaction with hydrophobic surfaces. In the present work we focused on the effect of alpha(s1)-casein on the fibrillogenesis of 1-40 beta-amyloid peptide, involved in Alzheimer's disease. Methods: The aggregation kinetics of beta-peptide in presence and absence of alpha(s1)-casein was followed under shear at 37 degrees C by recording the Thioflavine fluorescence, usually taken as an indicator of fibers formation. Measurements of Static and Dynamic Light Scattering, Circular Dichroism, and AFM imaging were done to reveal the details of alpha(s1)-casein-A beta(1-40) interaction. Results and discussions: alpha(s1)-Casein addition sizably increases the lag-time of the nucleation phase and slows down the entire fibrillization process. alpha(s1)-Casein sequesters the amyloid peptide on its surface thus exerting a chaperone-like activity by means a colloidal inhibition mechanism. General significance: Insights on the working mechanism of natural chaperones in preventing or controlling the amyloid aggregation.

Published
2012

47. Sucrose Pectin Interaction from Solution to Gels

Author

Bulone D., Giacomazza D., Manno M., Martorana V., and San Biagio P.L.

Abstract

Pectin is a very important polysaccharide in food technology, due to its ability to thicken or gel in aqueous solution under specific condition. One of the most common uses of pectin is in making jellies or jams, which requires the addition of a large amount of sucrose to acidic solutions. The role of sucrose in promoting pectin gelation has been ascribed to the strengthening of hydrophobic interaction consistently with its well-known stabilizing effect on protein structure. On the other hand, more specific effects on dimension and stiffness of pectin chains have been suggested by computational work. Here we present measurements of rheology, static and dynamic light scattering on samples of pectin containing different amounts of sucrose, ranging from few percent up to close the solubility limit of sucrose. This corresponds to spanning from low viscous liquid samples to strong gels. Results show that below the threshold value of 55% w/w, sucrose acts a critical parameter for the sol/gel transition by increasing the strength of excluded volume and hydrodynamic interaction between polymer chains. A further increase of sucrose above the critical concentration yields gels with a higher viscoelastic component corresponding to a higher amount of frozen structural inhomogeneities.

Published
2010

48. Slowdown of 1-40 beta-peptide aggregation by addition of two synthetic biocompatible polymers

Author

Sciortino P, Carrotta R, Cavallaro G, Bulone D, and San Biagio PL

Abstract

Fibril deposit formation of ainyloid P-protreiri (AP) iii the braiii is a liallmark oi Alzlieiiiicr disease (AD). Fibril: forination is triggered by 1nolecu1a.rc o~lformationacl hangeii and protein-protein interactions iiivolvirig partially unfo1de:i regioris of different AP peptide moleciiles. lncreasing cvi(.erice suggests that toxicity is linlced to diffusible AP oligoiners, which liave bccri foiind in soluble brain extracts of AI) patients, ratl-ier thail to the insoluble fibres. New thcrapcl tical approach, based 011 searchiiig molecules capable of regulating the peptide aggregation, is currently developiilg.

Published
2009

49. Applications of optical sensors to the detection of light scattered from gelling systems

Author

Bulone D., Manno M., San Biagio P.L., and Martorana V.

Abstract

Visible light, scattered within an angle of few degrees, (Small Angle Light Scattering, SALS) yields information on the spatial correlations and dynamical properties on the scale of the micrometers. In this way a quick and non-invasive characterization of a variety of samples is feasible. Lately the SALS instruments have been built around multielement optical sensors (CCD, CMOS), allowing the simultaneous measurement of the complete structure factor even during fast kinetics. An assessment of some sensor matrices of different technology will be presented. The macromolecular assemblies produced by polysaccharides or proteins can be functional or dysfunctional, their properties being either desirable or detrimental. Anyhow, their morphology often depends, in a very delicate way, on the presence of cosolutes, on the thermal history, on the biopolymer concentration etc. We present some applications of low angle dynamic and static light scattering to the study of gelling systems (agarose, pectin, insulin).

Published
2009

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