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.