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Abstract
Cα to N substitution in aza-amino acids imposes local conformational constraints, changes in hydrogen bonding properties, and leads to adaptive chirality at the nitrogen atom. These properties can be exploited in mimicry and stabilization of peptide secondary structures and self-assembly. Here, the effect of a single aza-amino acid incorporation located in the upper β-strand at a hydrogen-bonded (HB) site of a β-hairpin model peptide (H-Arg-Tyr-Val-Glu-Val-d-Pro-Gly-Orn-Lys-Ile-Leu-Gln-NH2) is reported. Specifically, analogs in which valine3 was substituted for aza-valine3 or aza-glycine3 were synthesized, and their β-hairpin stabilities were examined using Nuclear Magnetic Resonance (NMR) spectroscopy. The azapeptide analogs were found to destabilize β-hairpin formation compared to the parent peptide. The aza-valine3 residue was more disruptive of β-hairpin geometry than its aza-glycine3 counterpart.
Highlights
Introduction β-sheets are common protein secondary structures that are often involved in protein-protein interactions and protein aggregation [1,2]
In the pursuit of protein-protein interaction (PPI) inhibitors, β-strand and β-sheet peptidomimetics have been explored using a variety of unnatural scaffolds [4]
We expand the folding rules for aza-amino acids beyond turns and polyproline type II helices and characterize their effect on β-hairpin stability when incorporated into the β-strand region
Summary
Aza-amino acid acid (in (in blue) blue) creates creates one one face face with with increased increased hydrogen hydrogen bonding bonding properties properties and and one with reduced hydrogen bonding capacity.
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