Effects of incorporation of azido moieties into the hydrophobic core of coiled coil peptidesElectronic supplementary information (ESI) available: General peptide synthesis, procedures for CD measurements including spectra, DLS, TEM, FT-IR, and SEM measurements, confocal microscopy measurements including labelling of L4Z4 aggregates with FITC. See DOI: 10.1039/c4cc09089f

The secondary structure of the coiled coil peptides was regulated by altering the azido content at the hydrophobic core. These peptides were further investigated to form higher-order assemblies presumably via azido-mediated interactions. Controlled peptide folding via the variation of azido content.

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Bibliographic Details
Main Authors: Cheong, Jian Liang, Lim, Jaehong, Toh, Jerry K. C, Jee, Joo-Eun, Wong, Lan Li, Venkataraman, Shrinivas, Lee, Su Seong, Lee, Song-Gil
Format: Article
Language:English
Online Access:Get full text
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Summary:The secondary structure of the coiled coil peptides was regulated by altering the azido content at the hydrophobic core. These peptides were further investigated to form higher-order assemblies presumably via azido-mediated interactions. Controlled peptide folding via the variation of azido content.
ISSN:1359-7345
1364-548X
DOI:10.1039/c4cc09089f