Jump to main content
Jump to site search

Issue 18, 2013
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 12 May 2012, accepted on 19 Oct 2012 and first published on 02 Nov 2012


Article type: Communication
DOI: 10.1039/C2CC33432A
Citation: Chem. Commun., 2013,49, 1799-1801
  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements