Effects of incorporation of azido moieties into the hydrophobic core of coiled coil peptides

Abstract

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.

Formation of functional super-helical assemblies by constrained single heptad repeat

“…Several others peptides that have the propensity for helical super structure formation were designed by modifying the nature of hydrophobic amino acids in the core as well as the characteristics of the residual heptad positions. These designer building blocks self-assembled into distinct nanostructures having morphology ranging from fibres to net-like architectures to vesicles 22 23 24 25 26 27 . Here we describe for the first time the design and formation of a super-helical structure formed by the molecular self-assembly of a single heptad peptide sequence.…”