Transition of Nano-Architectures Through Self-Assembly of Lipidated β3-Tripeptide Foldamers.

ABSTRACT: β3-peptides consisting exclusively of β3-amino acids adopt a variety of non-natural helical structures and can self-assemble into well-defined hierarchical structures by axial head-to-tail self-assembly resulting in fibrous materials of varying sizes and shapes. To allow control of fiber morphology, a lipid moiety was introduced within a tri-β3-peptide sequence at each of the three amino acid positions and the N-terminus to gain finer control over the lateral assembly of fibers. Depending on the position of the lipid, the self-assembled structures formed either twisted ribbon-like fibers or distinctive multilaminar nanobelts. The nanobelt structures were comprised of multiple layers of peptide fibrils as revealed by puncturing the surface of the nanobelts with an AFM probe. This stacking p

SUBMITTER: Habila N 

PROVIDER: S-EPMC7136582 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature