Exploiting Cross-Amyloid Interactions To Inhibit Protein Aggregation but not Function: Nanomolar Affinity Inhibition of Insulin Aggregation by an IAPP Mimic

Laboratory of Peptide Biochemistry, Center for Integrated Protein Science München, Technische Universität München, An der Saatzucht 5, 85350 Freising-Weihenstephan, Germany.
Angewandte Chemie International Edition (Impact Factor: 11.26). 09/2008; 47(37):7114-8. DOI: 10.1002/anie.200801499
Source: PubMed


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.

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    • "It was shown that the so-called IAPP-GI peptide efficiently inhibits IAPP amyloid formation and cytotoxicity [13], [17]. More interestingly, IAPP-GI was demonstrated to block cytotoxic assembly of Aβ and insulin as well [18], [19]. The cross-association reaction between IAPP-GI (or nonfibrillar IAPP conformers) and Aβ may have some implications beyond its therapeutic potentials, and along with clinical and epidemiological evidences, provide a potential molecular link between AD and adult-onset diabetes [20]. "
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