Architectural control of rod-coil block polypeptide thermoresponsive self-assembly via de novo 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 control of the temperature of assembly based on the control of interactions between the ELP domains. Cryogenic transmission electron microscopy of assembled polypeptides confirmed distinct morphologies including core-shell particles and multilayer vesicles, depending on the parallel or antiparallel bundle architecture of the block polypeptide. The results highlight the potential for controlling multi-stimuli responsiveness and morphologies through fine control of the architectural features of the component polypeptide domains, with applications in materials design.