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. 2011 Apr 28;6(4):e19291. doi: 10.1371/journal.pone.0019291

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Santhoshkumar et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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In vivo αA-(66-80) peptides interact with crystallins and affect the structure and organization of crystallins, leading to age-related changes and cataract development. At low concentrations, αA-(66-80) specifically interacts with α-crystallin, resulting in increased hydrophobicity and polydispersity and decreased chaperone activity of α-crystallin. At higher concentrations, αA-(66-80) binds to crystallins, leading to insolubilization of crystallins and cataract development. Localized accumulation of the αA-(66-80) peptide has the potential to form light-scattering amyloid-like structures. However, the latter is less likely because the interaction of the peptide with crystallins suppresses the formation of fibrils.