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- W843422225 abstract "The demonstration of chaperone-like activity in peptides (mini-chaperones) derived from α-crystallin's chaperone region has generated significant interest in exploring the therapeutic potential of peptide chaperones in diseases of protein aggregation. Recent studies in experimental animals show that mini-chaperones could reach intended targets and alter the disease phenotype. Although mini-chaperones show potential benefits against protein aggregation diseases, they do tend to form aggregates on storage. There is thus a need to fine-tune peptide chaperones to increase their solubility, pharmacokinetics, and biological efficacy.This review summarizes the properties and the potential therapeutic roles of mini-chaperones in protein aggregation diseases and highlights some of the refinements needed to increase the stability and biological efficacy of mini-chaperones while maintaining or enhancing their chaperone-like activity against precipitation of unfolding proteins.Mini-chaperones suppress the aggregation of proteins, block amyloid fibril formation, stabilize mutant proteins, sequester metal ions, and exhibit antiapoptotic properties. Much work must be done to fine-tune mini-chaperones and increase their stability and biological efficacy. Peptide chaperones could have a great therapeutic value in diseases associated with protein aggregation and apoptosis.Accumulation of misfolded proteins is a primary cause for many age-related diseases, including cataract, macular degeneration, and various neurological diseases. Stabilization of native proteins is a logical therapeutic approach for such diseases. Mini-chaperones, with their inherent antiaggregation and antiapoptotic properties, may represent an effective therapeutic molecule to prevent the cascade of protein conformational disorders. Future studies will further uncover the therapeutic potential of mini-chaperones. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease." @default.
- W843422225 created "2016-06-24" @default.
- W843422225 creator A5039345178 @default.
- W843422225 creator A5053005998 @default.
- W843422225 creator A5075150530 @default.
- W843422225 date "2016-01-01" @default.
- W843422225 modified "2023-09-24" @default.
- W843422225 title "Alpha-crystallin-derived peptides as therapeutic chaperones" @default.
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- W843422225 doi "https://doi.org/10.1016/j.bbagen.2015.06.010" @default.
- W843422225 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4673008" @default.
- W843422225 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26141743" @default.
- W843422225 hasPublicationYear "2016" @default.
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