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Identification of Hot Regions of the Aβ–IAPP Interaction Interface as High‐Affinity Binding Sites in both Cross‐ and Self‐Association
Author(s) -
Andreetto Erika,
Yan LiMei,
TatarekNossol Marianna,
Velkova Aleksandra,
Frank Ronald,
Kapurniotu Aphrodite
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200904902
Subject(s) - islet , amyloid (mycology) , peptide , chemistry , identification (biology) , biochemistry , binding site , biophysics , biology , diabetes mellitus , endocrinology , inorganic chemistry , botany
Short peptide sequences are identified as hot regions of the cross‐interaction interface of the Alzheimer's disease β‐amyloid peptide (Aβ) with the type 2 diabetes islet amyloid polypeptide (IAPP). They are shown to be high‐affinity ligands of both Aβ and IAPP, thus suggesting common molecular recognition features in amyloid self‐ and cross‐amyloid hetero‐assembly.