Dynamic protein folding at the surface of stimuli-responsive peptide fibrils.

ABSTRACT: The repetitive self-assembled structure of amyloid can serve as inspiration to design functional materials. Herein, we describe the design of α/β6, a peptide that contains distinct α-helical and β-structure forming domains. The folding and association state of each domain can be controlled by temperature. At low temperatures, the α-domain favors a coiled-coil state while the β-domain is unstructured. Irreversible fibril formation via self-assembly of the β-domain is triggered at high temperatures where the α-domain is unfolded. Resultant fibrils serve as templates upon which reversible coiled coil formation of the α-domain can be thermally controlled. At concentrations of α/β6 ≥ 2.5 wt%, the peptide forms a mechanically defined hydrogel highlighting the possibility of designing materials w

SUBMITTER: Nagarkar RP 

PROVIDER: S-EPMC6032354 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature