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Factors responsible for the persistent adoption of hairpin conformations by hybrid oligopeptides, each having a central β/α dipeptide segment flanked by aromatic γ-amino acid (γAr) residues, are probed. Our recent studies revealed that tetrapeptide  1  and  2 , having central dipeptide segments consisting of β-alanine (β-Ala) and glycine (Gly), and L-β-homophenylalanine (L-β-homoPhe) and Gly residues, respectively, that are flanked by γAr residues, fold into well-defined, expanded β-turns with doubly H-bonded γAr residues. Replacing the γAr residues of  1  and  2  with L-Val and L-Leu residues results in tetrapetides  1  ′  and  2  ′  that fail to fold into defined conformations, which confirms the decisive role played by the H-bonded γAr residues in the promoting folding of  1  and  2 . Attaching L-Val and L-Leu residues to the termini of  1  affords hexapeptide  1a . With an additional H-bond between its L-Val and L-Leu residues, peptide  1a  folds into a hairpin with higher stability than that of  1 , indicating that the expanded β-turn can nucleate and stabilize β-hairpin with longer β-strands. Attaching L-Val and L-Leu residues to the termini of  2  affords hexapeptide  2a . Substituting the L-β-homoPhe residue of  2a  with a D-β-homoPhe residue gives hexapeptide  2b . Surprisingly, hexapeptide  2a  fold into a hairpin showing the similar stability as those of tetrapeptides  1  and  2 . Hexapeptide  2b , with its combination of a D-β-homoPhe residue and the L-Val/L-Leu pair, fold into a hairpin that is significantly more stable than the other hybrid peptides, demonstrating that a combination of hetero-chirality between the β-amino acid residue of the dipeptide loop and the α-amino acid residues of the β-strands enhances the stability of the resultant β-hairpin.

Major Factors for the Persistent Folding of Hybrid α, β, γ-Hybrid Peptides Into Hairpins