Modulation of Coiled-Coil Binding Strength and Fusogenicity through Peptide Stapling.

ABSTRACT: Peptide stapling is a technique which has been widely employed to constrain the conformation of peptides. One of the effects of such a constraint can be to modulate the interaction of the peptide with a binding partner. Here, a cysteine bis-alkylation stapling technique was applied to generate structurally isomeric peptide variants of a heterodimeric coiled-coil forming peptide. These stapled variants differed in the position and size of the formed macrocycle. C-terminal stapling showed the most significant changes in peptide structure and stability, with calorimetric binding analysis showing a significant reduction of binding entropy for stapled variants. This entropy reduction was dependent on cross-linker size and was accompanied by a change in binding enthalpy, illustrating the effects

SUBMITTER: Crone NSA 

PROVIDER: S-EPMC7086394 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature