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Exploiting Cross‐Amyloid Interactions To Inhibit Protein Aggregation but not Function: Nanomolar Affinity Inhibition of Insulin Aggregation by an IAPP Mimic
Author(s) -
Velkova Aleksandra,
TatarekNossol Marianna,
Andreetto Erika,
Kapurniotu Aphrodite
Publication year - 2008
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.200801499
Subject(s) - peptide , chemistry , amyloid (mycology) , protein aggregation , insulin , function (biology) , biochemistry , biophysics , amyloid fibril , amyloid β , microbiology and biotechnology , disease , biology , medicine , endocrinology , inorganic chemistry
Potential aggregate preventer : The designed peptide IAPP‐GI inhibits the non‐native aggregation of insulin without affecting its function. As the peptide also blocks aggregation of key amyloid peptides that occur in Alzheimer's disease and type II diabetes, it is a promising drug candidate.