Topological Study of the Structures of Heterochiral Peptides Containing Equal Amounts of l-Leu and d-Leu.

作者: Yosuke Demizu , Hiroko Yamashita , Mitsunobu Doi , Takashi Misawa , Makoto Oba

DOI: 10.1021/ACS.JOC.5B01541

关键词: StereochemistryProtein structureChemistryOligopeptidePeptideCrystallographyLeucineStereoisomerism

摘要: We designed and synthesized two dodecapeptides, Boc-(l-Leu-l-Leu-Aib-d-Leu-d-Leu-Aib)2-OMe (5) Boc-l-Leu-l-Leu-Aib-(d-Leu-d-Leu-Aib)2-l-Leu-l-Leu-Aib-OMe (6), that contain equal amounts of l-Leu, d-Leu, achiral Aib residues. The conformations peptides 5 6 in the crystalline state were studied using X-ray crystallographic analysis. Peptide formed a left-handed (M) α-helical structure, whereas peptide was composed combination fused right-handed (P) 310-helical structures. In solution, roughly equivalent helices present 5, α-helix as its dominant conformation.

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