Architectural control of rod-coil block polypeptide thermoresponsive self-assembly <i>via de novo</i> design of coiled-coil orientation.

ABSTRACT: The architectural control of the self-assembly of a series of block polypeptides comprising a concatenation of an elastin-like peptide and a coiled-coil, bundle-forming peptide (ELP-BFPs), has been demonstrated. Assembly of the polypeptides is controlled by coacervation of the hydrophobic ELP domain, while the type of coiled-coil assembly of the BFP and the specific placement of short histidine tags significantly tunes assembly behavior. Spectrophotometric analysis of self-assembly demonstrated that the transition temperature of assembly can be controlled by the design of the BFP domain and positioning of the His-tags in the constructs. Cryogenic transmission electron microscopy of assembled polypeptides confirmed distinct morphologies including core-shell particles and multilayer vesicles

SUBMITTER: Wang B 

PROVIDER: S-EPMC12054350 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature