Self-Assembly of Aromatic Amino Acid Enantiomers into Supramolecular Materials of High Rigidity.

ABSTRACT: Most natural biomolecules may exist in either of two enantiomeric forms. Although in nature, amino acid biopolymers are characterized by l-type homochirality, incorporation of d-amino acids in the design of self-assembling peptide motifs has been shown to significantly alter enzyme stability, conformation, self-assembly behavior, cytotoxicity, and even therapeutic activity. However, while functional metabolite assemblies are ubiquitous throughout nature and play numerous important roles including physiological, structural, or catalytic functions, the effect of chirality on the self-assembly nature and function of single amino acids is not yet explored. Herein, we investigated the self-assembly mechanism of amyloid-like structure formation by two aromatic amino acids, phenylalanine (Phe) an

SUBMITTER: Bera S 

PROVIDER: S-EPMC7123433 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature