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• W1468403291 startingPage "8597" @default.
• W1468403291 abstract "We designed and synthesized two dodecapeptides, Boc-(l-Leu-l-Leu-Aib-d-Leu-d-Leu-Aib)2-OMe (5) and 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, and achiral Aib residues. The conformations of peptides 5 and 6 in the crystalline state were studied using X-ray crystallographic analysis. Peptide 5 formed a left-handed (M) α-helical structure, whereas peptide 6 was composed of a combination of fused (M) α-helical and right-handed (P) 310-helical structures. In solution, roughly equivalent amounts of (P) and (M) helices were present in 5, whereas the (M) α-helix was present in 6 as its dominant conformation." @default.
• W1468403291 created "2016-06-24" @default.
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• W1468403291 date "2015-08-22" @default.
• W1468403291 modified "2023-09-28" @default.
• W1468403291 title "Topological Study of the Structures of Heterochiral Peptides Containing Equal Amounts of <scp>l</scp>-Leu and <scp>d</scp>-Leu" @default.
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• W1468403291 doi "https://doi.org/10.1021/acs.joc.5b01541" @default.
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