A Change in the 310- to α-Helical Transition Point in the Heptapeptides Containing Sulfur and Selenium

Crystal structures of three heptapeptides Boc-Ala-Leu-Aib-XXX-Ala-Leu-Aib-OMe (where XXX = methionine in peptide A, selenomethionine in peptide B, and S- benzyl cysteine in peptide C) reveal mixed 310-/α-helical conformations with R factors of 6.94, 5.79, and 5.98, respectively. All the structures were solved in the P212121 space group. 310- to α-helical transitions are observed in all of these peptides. The helices begin as a 310-helical segment at the N-terminus and then transit for peptides A and C at residue Aib(3) carbonyl (O(3)), while for peptide B the transition occurs at residue Leu(2) carbonyl oxygen (O(2)). There are water molecules associated in the crystal of each of these peptides and they form different types of hydrogen bonding patterns in each crystal. The observations suggest that 310- to α-helical transition is sequence dependent in these short heptapeptide sequences.