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Peptide Inhibitors of the amyloidogenesis of IAPP : verification of the hairpin‐binding geometry hypothesis
Author(s) -
Sivanesam Kalkena,
Shu Irene,
Huggins Kelly N. L.,
TatarekNossol Marianna,
Kapurniotu Aphrodite,
Andersen Niels H.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12261
Subject(s) - peptide , chemistry , biophysics , stereochemistry , biochemistry , biology
Versions of a previously discovered β‐hairpin peptide inhibitor of IAPP aggregation that are stabilized in that conformation, or even forced to remain in the hairpin conformation by a backbone cyclization constraint, display superior activity as inhibitors. The cyclized hairpin, cyclo‐ WW 2, displays inhibitory activity at substoichiometric concentrations relative to this amyloidogenic peptide. The hairpin‐binding hypothesis stands confirmed.