Peptide catalysts often incorporate secondary structure, which may benefit catalysis by spatially positioning catalytic residues. We have been studying how β-hairpin secondary structure influences the activity of ester hydrolysis catalysts. We monitored the hydrolysis of <i>para</i>-nitrophenyl acetate (pNPA) with a number of peptide catalysts. The peptide catalysts were designed from a tryptophan zipper scaffold that incorporated catalytic histidine residues. Each β-hairpin catalytic peptide was compared to a near-identical analogue that lacked β-hairpin character. With this scaffold, we found that the peptides lacking β-hairpin character were more active catalysts. Other scaffolds are now being used instead to further explore the role of secondary structure on catalysis.

Role of secondary structure in ester hydrolysis catalytic peptides

ACS Spring 2022

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