Trichromophoric pentapeptide: impact of β-sheet conformation on dual path to excimer emission and sensing of BSA

Abstract

We are reporting two mechanisms for excimer emission in a designed trichromophoric pentapeptide wherein the triazolo aromatic amino acid scaffold (^ArTAA) nucleates β-sheet conformation. The designed unnatural fluorescent pentapeptide shows an excimer emission either via FRET from the scaffold (^ArTAA) acting as a donor or via direct excitation of an acceptor chromophore, ^TPyAla_Do. Moreover, it serves as an effective fluorescence light-up probe for studying protein–peptide interactions.