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Chem Commun (Camb). 2013 Mar 4;49(18):1799-801. doi: 10.1039/c2cc33432a. Epub 2012 Nov 12.

Characterizing the assembly behaviors of human amylin: a perspective derived from C-terminal variants.

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1
Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China.

Abstract

The differences in the C-terminal domains of human amylin peptide variants initiate different aggregation processes and differences in the composition of the aggregates by affecting the hydrophobic cores, conformations, and intra-sheet interactions of the peptides, which have distinct effects on the cytotoxicity of the peptides.

PMID:
23146899
DOI:
10.1039/c2cc33432a
[Indexed for MEDLINE]
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