Conformational modulation of peptides using β-amino benzenesulfonic acid (SAnt)

Abstract

This communication describes the utility of a conformationally restricted aromatic β-amino acid (2-aminobenzenesulfonic acid, ^SAnt) inducing various folding interactions in short peptides. Sandwiching ^SAnt between diverse amino acid residues was shown to form robust folded architectures featuring a variety of H-bonded networks, suggesting its utility in inducing peptide folding.