Sequence-Dependent Nanofiber Structures of Phenylalanine and Isoleucine Tripeptides.

ABSTRACT: The molecular design of short peptides to achieve a tailor-made functional architecture has attracted attention during the past decade but remains challenging as a result of insufficient understanding of the relationship between peptide sequence and assembled supramolecular structures. We report a hybrid-resolution model to computationally explore the sequence-structure relationship of self-assembly for tripeptides containing only phenylalanine and isoleucine. We found that all these tripeptides have a tendency to assemble into nanofibers composed of laterally associated filaments. Molecular arrangements within the assemblies are diverse and vary depending on the sequences. This structural diversity originates from (1) distinct conformations of peptide building blocks that lead to differen

SUBMITTER: Xiong Q 

PROVIDER: S-EPMC7696242 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature