Catalytically active peptides affected by self-assembly and residues order

• Designed peptides showed a link between catalytic amino acids order and activity. Side chains engaged in stabilizing may become inaccessible to catalysis. Structural characterizations do provide insights on catalysis by peptide assemblies. Amphiphilic that induce are interesting alternatives natural enzymes thanks robustness of their synthesis the ability certain types conformations specific motifs acid sequences. Various studies aimed at mimicking activity serine proteases designed peptides. Here we demonstrate which triad residues positioned along amphiphilic β-strands influences both assembly structures A set three β-sheet peptides, decorated with different orders acids, Glu, His Ser strands were evaluated for hydrolysis efficiency p -nitrophenyl acetate ( NPA) substrate. Among Ac-Cys-Phe-Glu-Phe-Ser-Phe-His-Phe-Pro-NH 2 (ESH) achieved greatest value 0.19 M −1 s , concentration 250 μM. This study sheds light an overlooked factor designing assemblies whereby charged make up active sites, fact intermolecular interactions turn hamper action.