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Molecular Mapping of the Recognition Interface between the Islet Amyloid Polypeptide and Insulin
Author(s) -
Gilead Sharon,
Wolfenson Haguy,
Gazit Ehud
Publication year - 2006
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.200602034
Subject(s) - islet , amyloid (mycology) , peptidomimetic , insulin , mechanism (biology) , chemistry , computational biology , biochemistry , neuroscience , endocrinology , biology , philosophy , peptide , inorganic chemistry , epistemology
Nature's route for amyloid prevention : Insulin is a natural inhibitor of amyloid formation by the islet amyloid polypeptide (IAPP). The interacting domains of both proteins were identified by using a reductionist approach (see scheme). An understanding of the molecular mechanism of this physiological interaction may lead to the design of peptidomimetic drugs for type II diabetes.