Journal
JOURNAL OF PEPTIDE RESEARCH
Volume 57, Issue 5, Pages 428-434Publisher
WILEY
DOI: 10.1034/j.1399-3011.2001.00871.x
Keywords
beta-sheet; chaperone; mini-alpha A-crystallin
Funding
- NEI NIH HHS [EY11981] Funding Source: Medline
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The chaperone activity and biophysical properties of the 19 amino acid peptide DFVIFLDVKHFSPEDLTVK, identified as the functional element in alphaA-crystallin and here referred to as mini-alphaA-crystallin, were studied using light scattering and spectroscopic methods after altering its sequence and enantiomerism. The all-D and all-L conformers of the peptide do not show marked differences in their chaperone-like activity against heat-induced aggregation of alcohol dehydrogenase at 48 degreesC and dithiothreitol-induced aggregation of insulin. The retro peptide does not show any secondary structure and is also unable to act like a chaperone. Both all-L and all-D peptides lose their beta -sheet conformations, hydrophobicity and chaperone-like activity at temperatures > 50 degreesC. However, upon cooling, a significant portion of those properties was regained, suggesting temperature-dependent, reversible structural alterations in the peptides under investigation. We propose that both the hydrophobicity and beta -sheet conformation of the functional element of alphaA-crystallin are essential for chaperone-like activity.
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