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

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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Published inAngewandte Chemie International Edition Vol. 47; no. 37; pp. 7114 - 7118
Main Authors Velkova, Aleksandra, Tatarek-Nossol, Marianna, Andreetto, Erika, Kapurniotu, Aphrodite
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 01.09.2008
WILEY‐VCH Verlag
Subjects
Amino Acid Sequence
Amyloid - antagonists & inhibitors
Amyloid - chemistry
Amyloid - metabolism
Amyloid - pharmacology
Amyloid - toxicity
Cell Line, Tumor
diabetes
Humans
insulin
Insulin - metabolism
islet amyloid polypeptide
Molecular Mimicry
Molecular Sequence Data
protein aggregation
protein design
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Summary: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.
Bibliography:We are grateful to S. Stevanovic and C. Henkel for MALDI measurements, J. Bernhagen for help in establishing the insulin receptor assays, and L. M. Yan for helpful discussions and preliminary studies on insulin fibrillization. This work was supported by the Deutsche Forschungsgemeinschaft (DFG).
ark:/67375/WNG-X0PMC58V-6
Deutsche Forschungsgemeinschaft
istex:2FB8853900AFA927653B2A9F23CDFCB302287418
ArticleID:ANIE200801499
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200801499