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Macromoleculemediated Chaperoning Function In Vivo And Its Implications In The Protein Aggregation-associated Problems | 8243
ISSN: 0975-0851

Journal of Bioequivalence & Bioavailability
Open Access

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Macromoleculemediated chaperoning function in vivo and its implications in the protein aggregation-associated problems

2nd World Congress on Bioavailability & Bioequivalence: Pharmaceutical R & D Summit-2011 and International Conference on Pharmaceutics & Novel Drug Delivery Systems

Seongil Choi

ScientificTracks Abstracts: JBB

DOI: 10.4172/2153-2435.10000S4

P roteins frequently encounter misfolding and aggregation during their biogenesis and their life cycles in the cell. Importantly, protein aggregation is closely associated with many of debilitating neurodegenerative disorders, including Alzheimer?s disease, Parkinson?s disease, Huntington?s disease and prion-caused diseases. Th us, the understanding of protein aggregation in vivo in terms of chaperoning function has been of great importance in modern biology. Th e molecular chaperones such as HSP60 and HSP70 have been widely believed to assist protein folding by preventing aggregation via transient binding to the exposed hydrophobic regions of non-native substrates. Nevertheless, most proteins can fold without their assistance in vivo. Traditionally, hydrophobic interaction-mediated substrate recognition and stabilization against aggregation have provided a conceptual framework for the understanding of the action mechanism of molecular chaperones. In contrast, my recent research has shown that the surface charges (probably resulting in electrostatic repulsions) and steric hindrance of macromolecules (ribosomes, RNA, and molecular chaperones as well) interacting with aggregationprone proteins could be key factors responsible for preventing aggregation. Of note, this proposed mechanism is fundamentally diff erent from the prevailing hydrophobic interaction-mediated stabilization against aggregation, thus giving new insights into our understanding of protein aggregation in terms of chaperoning function in vivo . Furthermore, the implications of my research in the above protein aggregation problems will be presented
Seongil Choi has completed his Ph.D in 2004 and postdoctoral studies from Yonsei, University. He is a research professor at Yonsei University. He has published 11 papers in reputed journals. His research has been aimed at elucidating the chaperoning roles of macromolecules interacting with proteins during de novo folding in vivo