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4. Human Plasma Protein Corona of Aβ Amyloid and Its Impact on Islet Amyloid Polypeptide Cross-Seeding

Author

Nandakumar, Aparna, primary, Xing, Yanting, additional, Aranha, Ritchlynn R., additional, Faridi, Ava, additional, Kakinen, Aleksandr, additional, Javed, Ibrahim, additional, Koppel, Kairi, additional, Pilkington, Emily H., additional, Purcell, Anthony Wayne, additional, Davis, Thomas P., additional, Faridi, Pouya, additional, Ding, Feng, additional, and Ke, Pu Chun, additional

Published
2020
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5. Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide

Author

Kakinen, Aleksandr, Xing, Yanting, Hegoda Arachchi, Nuwan Dhanushka, Javed, Ibrahim, Feng, Lei, Faridi, Ava, Douek, Alon M, Sun, Yunxiang, Kaslin, Jan, Davis, Thomas P, Higgins, Michael J, Ding, Feng, Ke, Pu Chun, Kakinen, Aleksandr, Xing, Yanting, Hegoda Arachchi, Nuwan Dhanushka, Javed, Ibrahim, Feng, Lei, Faridi, Ava, Douek, Alon M, Sun, Yunxiang, Kaslin, Jan, Davis, Thomas P, Higgins, Michael J, Ding, Feng, and Ke, Pu Chun

Abstract

Human amyloids and plaques uncovered post mortem are highly heterogeneous in structure and composition, yet literature concerning the heteroaggregation of amyloid proteins is extremely scarce. This knowledge deficiency is further exacerbated by the fact that peptide delivery is a major therapeutic strategy for targeting their full-length counterparts associated with the pathologies of a range of human diseases, including dementia and type 2 diabetes (T2D). Accordingly, here we examined the coaggregation of full-length human islet amyloid polypeptide (IAPP), a peptide associated with type 2 diabetes, with its primary and secondary amyloidogenic fragments 19-29 S20G and 8-20. Single-molecular aggregation dynamics was obtained by high-speed atomic force microscopy, augmented by transmission electron microscopy, X-ray diffraction, and super-resolution stimulated emission depletion microscopy. The coaggregation significantly prolonged the pause phase of fibril elongation, increasing its dwell time by 3-fold. Surprisingly, unidirectional elongation of mature fibrils, instead of protofilaments, was observed for the coaggregation, indicating a new form of tertiary protein aggregation unknown to existing theoretical models. Further in vivo zebrafish embryonic assay indicated improved survival and hatching, as well as decreased frequency and severity of developmental abnormalities for embryos treated with the heteroaggregates of IAPP with 19-29 S20G, but not with 8-20, compared to the control, indicating the therapeutic potential of 19-29 S20G against T2D.

Published
2019

7. Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide

Author

Kakinen, Aleksandr, primary, Xing, Yanting, additional, Hegoda Arachchi, Nuwan, additional, Javed, Ibrahim, additional, Feng, Lei, additional, Faridi, Ava, additional, Douek, Alon M., additional, Sun, Yunxiang, additional, Kaslin, Jan, additional, Davis, Thomas P., additional, Higgins, Michael J., additional, Ding, Feng, additional, and Ke, Pu Chun, additional

Published
2019
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10. Mitigating Human IAPP Amyloidogenesis In Vivo with Chiral Silica Nanoribbons

Author

Faridi, Ava, primary, Sun, Yunxiang, additional, Okazaki, Yutaka, additional, Peng, Guotao, additional, Gao, Jie, additional, Kakinen, Aleksandr, additional, Faridi, Pouya, additional, Zhao, Mei, additional, Javed, Ibrahim, additional, Purcell, Anthony W., additional, Davis, Thomas P., additional, Lin, Sijie, additional, Oda, Reiko, additional, Ding, Feng, additional, and Ke, Pu Chun, additional

Published
2018
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14. Nanoparticle–proteome in vitro and in vivo

Author

Wang, Miaoyi, primary, Gustafsson, Ove J. R., additional, Pilkington, Emily H., additional, Kakinen, Aleksandr, additional, Javed, Ibrahim, additional, Faridi, Ava, additional, Davis, Thomas P., additional, and Ke, Pu Chun, additional

Published
2018
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15. Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide

Author

Kakinen, Aleksandr, Xing, Yanting, Hegoda Arachchi, Nuwan, Javed, Ibrahim, Feng, Lei, Faridi, Ava, Douek, Alon M., Sun, Yunxiang, Kaslin, Jan, Davis, Thomas P., Higgins, Michael J., Ding, Feng, and Ke, Pu Chun

Abstract

Human amyloids and plaques uncovered post mortem are highly heterogeneous in structure and composition, yet literature concerning the heteroaggregation of amyloid proteins is extremely scarce. This knowledge deficiency is further exacerbated by the fact that peptide delivery is a major therapeutic strategy for targeting their full-length counterparts associated with the pathologies of a range of human diseases, including dementia and type 2 diabetes (T2D). Accordingly, here we examined the coaggregation of full-length human islet amyloid polypeptide (IAPP), a peptide associated with type 2 diabetes, with its primary and secondary amyloidogenic fragments 19–29 S20G and 8–20. Single-molecular aggregation dynamics was obtained by high-speed atomic force microscopy, augmented by transmission electron microscopy, X-ray diffraction, and super-resolution stimulated emission depletion microscopy. The coaggregation significantly prolonged the pause phase of fibril elongation, increasing its dwell time by 3-fold. Surprisingly, unidirectional elongation of mature fibrils, instead of protofilaments, was observed for the coaggregation, indicating a new form of tertiary protein aggregation unknown to existing theoretical models. Further in vivo zebrafish embryonic assay indicated improved survival and hatching, as well as decreased frequency and severity of developmental abnormalities for embryos treated with the heteroaggregates of IAPP with 19–29 S20G, but not with 8–20, compared to the control, indicating the therapeutic potential of 19–29 S20G against T2D.

Published
2024
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16. Nanoparticle--proteome in vitro and in vivo.

Author

Miaoyi Wang, Gustafsson, Ove J. R., Pilkington, Emily H., Kakinen, Aleksandr, Javed, Ibrahim, Faridi, Ava, Davis, Thomas P., and Pu Chun Ke

Abstract

The protein corona is a concept central to a range of disciplines exploiting the bio--nano interface. As the literature continues to expand in this field, it is essential to condense and contextualize the in vitro and in vivo proteome databases accumulated over the past decade: a goal which this review intends to achieve for the benefit of nanomedicine and nanobiotechnology. The parameters used for our review are the physicochemical characteristics of the nanoparticles, their surface ligands, the biological matrix from which a corona was formed, methods employed, plus the top-ten enriched corona proteins. In addition, the protein coronal networks and their implications in vivo are highlighted for selected studies. [ABSTRACT FROM AUTHOR]

Published
2018
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19. Nanoparticle-proteome in vitro and in vivo

Author

Emily H. Pilkington, Ava Faridi, Thomas P. Davis, Aleksandr Kakinen, Ove J. R. Gustafsson, Ibrahim Javed, Pu Chun Ke, Miaoyi Wang, Wang, Miaoyi, Gustafsson, Ove JR, Pilkington, Emily H, Kakinen, Aleksandr, Javed, Ibrahim, Faridi, Ava, Davis, Thomas P, and Ke, Pu Chun

Subjects
endocrine system, Chemistry, Biomedical Engineering, Nanoparticle, Protein Corona, Nanotechnology, 02 engineering and technology, General Chemistry, General Medicine, in-vitro, 010402 general chemistry, 021001 nanoscience & nanotechnology, Proteomics, 01 natural sciences, In vitro, 0104 chemical sciences, In vivo, Proteome, medical nanotechnology, Nanobiotechnology, Nanomedicine, nanoparticles, General Materials Science, 0210 nano-technology
Abstract

The protein corona is a concept central to a range of disciplines exploiting the bio–nano interface. As the literature continues to expand in this field, it is essential to condense and contextualize the in vitro and in vivo proteome databases accumulated over the past decade: a goal which this review intends to achieve for the benefit of nanomedicine and nanobiotechnology. The parameters used for our review are the physicochemical characteristics of the nanoparticles, their surface ligands, the biological matrixfrom which a corona was formed, methods employed, plus the top-ten enriched corona proteins. In addition, the protein coronal networks and their implications in vivo are highlighted for selected studies. Refereed/Peer-reviewed

Published
2020

20. Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide

Author

Paul Wilson, Ava Faridi, Thomas P. Davis, Cleidi Zampronio, Pu Chun Ke, Juan Ramon Hernandez-Fernaud, Yanting Xing, Ove J. R. Gustafsson, Aleksandr Kakinen, Feng Ding, Emily H. Pilkington, Pilkington, Emily H, Gustafsson, Ove JR, Xing, Yanting, Hernandez-Fernaud, Juan, Zampronio, Cleidi, Kakinen, Aleksandr, Faridi, Ava, Ding, Feng, Wilson, Paul, Ke, Pu Chun, and Davis, Thomas P

Subjects
0301 basic medicine, endocrine system, Amyloid, Serum protein, General Physics and Astronomy, Protein Corona, 02 engineering and technology, Fibril, Article, RS, 03 medical and health sciences, protein corona, In vivo, Humans, liquid chromatography, General Materials Science, amyloidogenesis, Particle Size, mass spectrometry, geography, geography.geographical_feature_category, Chemistry, General Engineering, amyloid, Quartz crystal microbalance, 021001 nanoscience & nanotechnology, Islet, QP, Islet Amyloid Polypeptide, 030104 developmental biology, Quartz Crystal Microbalance Techniques, Biophysics, 0210 nano-technology, Fetal bovine serum
Abstract

Amyloids may be regarded as native nanomaterials that form in the presence of complex protein mixtures. By drawing an analogy with the physicochemical properties of nanoparticles in biological fluids, we hypothesized that amyloids should form a protein corona in vivo that would imbue the underlying amyloid with a modified biological identity. To explore this hypothesis, we characterized the protein corona of human islet amyloid polypeptide (IAPP) fibrils in fetal bovine serum using two complementary methodologies developed herein: quartz crystal microbalance and "centrifugal capture", coupled with nanoliquid chromatography tandem mass spectroscopy. Clear evidence for a significant protein corona was obtained. No trends were identified for amyloid corona proteins based on their physicochemical properties, whereas strong binding with IAPP fibrils occurred for linear proteins or multidomain proteins with structural plasticity. Proteomic analysis identified amyloid-enriched proteins that are known to play significant roles in mediating cellular machinery and processing, potentially leading to pathological outcomes and therapeutic targets. Refereed/Peer-reviewed

Published
2018
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