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Issue 18, 2013
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Characterizing the assembly behaviors of human amylin: a perspective derived from C-terminal variants

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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.

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

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Article information


Submitted
12 May 2012
Accepted
19 Oct 2012
First published
02 Nov 2012

Chem. Commun., 2013,49, 1799-1801
Article type
Communication

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

M. Chen, D. Zhao, Y. Yu, W. Li, Y. Chen, Y. Zhao and Y. Li, Chem. Commun., 2013, 49, 1799
DOI: 10.1039/C2CC33432A

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