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A comparative study of the impact of small, medium-sized, and bulky α,β-dehydroamino acids (ΔAAs) on the structure and stability of Balaram's incipient 3 10 -helical peptide ( 1 ) is reported. Replacement of the N -terminal Aib residue of 1 with a ΔAA afforded peptides 2a - c that maintained the 3 10 -helical shape of 1 . In contrast, installation of a ΔAA in place of Aib-3 yielded peptides 3a - c that preferred a β-sheet-like conformation. The impact of the ΔAA on peptide structure was independent of size, with small (ΔAla), medium-sized ( Z -ΔAbu), and bulky (ΔVal) ΔAAs exerting similar effects. The proteolytic stabilities of 1 and its analogs were determined by incubation with Pronase. Z-ΔAbu and ΔVal increased the resistance of peptides to proteolysis when incorporated at the 3-position and had negligible impact on stability when placed at the 1-position, whereas ΔAla-containing peptides degraded rapidly regardless of position. Exposure of peptides 2a - c and 3a - c to the reactive thiol cysteamine revealed that ΔAla-containing peptides underwent conjugate addition at room temperature, while Z -ΔAbu- and ΔVal-containing peptides were inert even at elevated temperatures. These results suggest that both bulky and more accessible medium-sized ΔAAs should be valuable tools for bestowing rigidity and proteolytic stability on bioactive peptides.

Impact of Dehydroamino Acids on the Structure and Stability of Incipient 310-Helical Peptides

Impact of Dehydroamino Acids on the Structure and Stability of Incipient 3₁₀-Helical Peptides