Arginine Methylation Regulates Self-Assembly of Peptides

Abstract

Bio-inspired design of peptides represents one facile strategy for development of supramolecular monomers for self-assembly into well-defined nanostructures. Inspired by methylation of arginine during post-translational modification for manipulating protein functions, herein, the controllable self-assembly of peptides via rational incorporation of methylated arginine residues into bola-amphiphilic peptides is reported. A series of bola-amphiphilic peptides are designed and synthesized either containing natural arginine or methylated arginine and investigate the influence of arginine methylation on peptide assembly. This study finds that incorporation of symmetrically di-methylated arginine into oppositely charged hexapeptide hex-SDMAE leads to distinct assembling performance compare to natural peptide hex-RE. The findings demonstrate that the methylation of rationally designed peptide sequences allows for regulation of self-assembly of peptides, thus implying the great potential of arginine methylation in establishing controllable peptide assembling systems and creating in situ formulation of biomedical materials in the future.

Keywords: arginine methylation; nanostructures; peptides; self-assembly; stimulus-responsiveness.