Exchange, promiscuity, and orthogonality in de novo designed coiled-coil peptide assemblies.

ABSTRACT: De novo protein design is delivering new peptide and protein structures at a rapid pace. Many of these synthetic polypeptides form well-defined and hyperthermal-stable structures. Generally, however, less is known about the dynamic properties of the de novo designed structures. Here, we explore one aspect of dynamics in a series of de novo coiled-coil peptide assemblies: namely, peptide exchange within and between different oligomers from dimers through to heptamers. First, we develop a fluorescence-based reporter assay for peptide exchange that is straightforward to implement, and, thus, would be useful to others examining similar systems. We apply this assay to explore both homotypic exchange within single species, and heterotypic exchange between coiled coils of dif

SUBMITTER: Kurgan KW 

PROVIDER: S-EPMC11664599 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature