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Your search keyword '"Agić, Dejan"' showing total 4 results
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1. Contributors

Author

Abraham, Soniya, primary, Abramić, Marija, additional, Adnan, Mohammed, additional, Agić, Dejan, additional, Ağrı, İbrahim, additional, Ağrı, Arzu Erdal, additional, Aguiar, Odair, additional, Aiello, Francesca, additional, Allgrove, Judith E, additional, Astiz, Susana, additional, Badolato, Mariateresa, additional, Bakir, Sena, additional, Baliga, Manjeshwar Shrinath, additional, Banerjee, Antara, additional, Banerjee, Anushka, additional, Barnes, Stephen, additional, Bissi, Laura, additional, Bruno, Antonio, additional, Calhau, Conceição, additional, Capanoglu, Esra, additional, Carullo, Gabriele, additional, Celep, Gulcin Sagdicoglu, additional, Christensen, Lars Porskjær, additional, Čvorović, Jovana, additional, D’Archivio, Massimo, additional, D’Cunha, Ritesh, additional, Davison, Glen, additional, D'souza, Reshmina, additional, Elrod, Susan M., additional, Erukainure, Ochuko L., additional, Faria, Ana, additional, Fernandes, Eduarda, additional, Fornasaro, Stefano, additional, Freitas, Marisa, additional, Garcia-Contreras, Consolacion, additional, George, Thomas, additional, Giovannini, Claudio, additional, Gollücke, Andréa Pittelli Boiago, additional, Gonzalez-Bulnes, Antonio, additional, Graier, Wolfgang F., additional, Guo, Honghui, additional, Guo, Tai L., additional, Harlen, Winda Christina, additional, Hölzel, Nadine, additional, Huang, Guannan, additional, Isabel, Beatriz, additional, Shahidul Islam, Md., additional, Jaffe, Russell, additional, Jati, Ignasius Radix A.P., additional, Kamiloglu, Senem, additional, Keating, Elisa, additional, Kent, Katherine, additional, Kesavan, Pallavi, additional, Kojima-Yuasa, Akiko, additional, Madreiter-Sokolowski, Corina T., additional, Mani, Jayashree, additional, Marotta, Francesco, additional, Martel, Fátima, additional, Masella, Roberta, additional, Mathai, Naveen Joseph, additional, Murugesan, Ramachandran, additional, Muscatello, Maria Rosaria Anna, additional, Naik, Taresh Shekar, additional, Özdemir, Doğukan, additional, Özgür, Abdulkadir, additional, Pais, Michael L.J., additional, Palatty, Princy Louis, additional, Passamonti, Sabina, additional, Pathak, Surajit, additional, Peres, Rogério Correa, additional, Popov, O.S., additional, Prasain, Jeevan K., additional, Rao, Suresh, additional, Rastija, Vesna, additional, Ribeiro, Daniel Araki, additional, Ribeiro, Daniela, additional, Saldanha, Elroy, additional, Sanni, Olakunle, additional, Scazzocchio, Beatrice, additional, Shalamay, A.S., additional, Shebeko, S.K., additional, Shimazu, Yoshihito, additional, Shivashankara, Arnadi Ramachandrayya, additional, Silenzi, Annalisa, additional, Simon, Paul, additional, Soumia, Bouzidi, additional, Sujayendra, Davanagere Murali, additional, Swarts, Nigel, additional, Takeda, Mamoru, additional, Takehana, Shiori, additional, Tarasenko, O.O., additional, Tomas, Merve, additional, Tramer, Federica, additional, Vazquez-Gomez, Marta, additional, Vuković, Rosemary, additional, Ward, Wendy E., additional, Michael Wyss, J., additional, Xia, Min, additional, Xu, Joella, additional, Yumol, Jenalyn L., additional, Ziberna, Lovro, additional, Zoccali, Rocco Antonio, additional, and Zupanets, I.A., additional

Published
2018
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3. Absolutely conserved tryptophan in M49 family of peptidases contributes to catalysis and binding of competitive inhibitors.

Author

Spoljarić J, Salopek-Sondi B, Makarević J, Vukelić B, Agić D, Simaga S, Jajcanin-Jozić N, and Abramić M

Subjects
Amino Acid Sequence, Binding, Competitive, Biocatalysis, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases antagonists & inhibitors, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases isolation & purification, Enzyme Inhibitors chemical synthesis, Enzyme Inhibitors chemistry, Humans, Hydroxamic Acids chemical synthesis, Hydroxamic Acids chemistry, Kinetics, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutant Proteins antagonists & inhibitors, Mutant Proteins isolation & purification, Mutant Proteins metabolism, Protein Stability, Sequence Homology, Amino Acid, Substrate Specificity, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases metabolism, Tryptophan chemistry
Abstract

The role of the unique fully conserved tryptophan in metallopeptidase family M49 (dipeptidyl peptidase III family) was investigated by site-directed mutagenesis on human dipeptidyl peptidase III (DPP III) where Trp300 was subjected to two substitutions (W300F and W300L). The mutant enzymes showed thermal stability equal to the wild-type DPP III. Conservative substitution of the Trp300 with phenylalanine decreased enzyme activity 2-4 fold, but did not significantly change the K(m) values for two dipeptidyl 2-naphthylamide substrates. However, the K(m) for the W300L mutant was elevated 5-fold and the k(cat) value was reduced 16-fold with Arg-Arg-2-naphthylamide. Both substitutions had a negative effect on the binding of two competitive inhibitors designed to interact with S1 and S2 subsites. These results indicate the importance of the aromatic nature of W300 in DPP III ligand binding and catalysis, and contribution of this residue in maintaining the functional integrity of this enzyme's S2 subsite.

Published
2009
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4. Novel amidino-substituted benzimidazoles: synthesis of compounds and inhibition of dipeptidyl peptidase III.

Author

Agić D, Hranjec M, Jajcanin N, Starcević K, Karminski-Zamola G, and Abramić M

Subjects
Adamantane analogs & derivatives, Adamantane pharmacology, Algorithms, Amides chemistry, Chemical Phenomena, Chemistry, Physical, Erythrocytes drug effects, Erythrocytes enzymology, Kinetics, Models, Molecular, Molecular Conformation, Structure-Activity Relationship, Benzimidazoles chemical synthesis, Benzimidazoles pharmacology, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases antagonists & inhibitors, Protease Inhibitors chemical synthesis, Protease Inhibitors pharmacology
Abstract

Dipeptidyl peptidase III (DPP III), also known as enkephalinase B, is a zinc-hydrolase with an indicated role in the mammalian pain modulatory system. In order to find a potent antagonist of this enzyme, we synthesized and screened the effect of a small set of benzimidazole derivatives on its activity. To improve the inhibitory potential, a cyclobutane ring was introduced as rigid conformation support to the diamidino substituted dibenzimidazoles. Two such compounds (1' and 4') from the group of cyclobutane derivatives containing amidino-substituted benzimidazole moieties, obtained by photochemical cyclization in water and by respecting rules of the "green chemistry" approach, were found to be strong DPP III inhibitors, with IC(50) value below 5 microM. Compound 1' displayed time-dependent inhibition towards human DPP III, characterized by the second-order rate constant of 6924+/-549 M(-1)min(-1) (K(i)=0.20 microM). The peptide substrate valorphin protected the enzyme from inactivation by 1'.

Published
2007
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