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A dodecapeptide, Boc‐( L ‐Leu‐ L ‐Leu‐Aib‐ L ‐Leu‐ D ‐Leu‐Aib) 2 ‐OMe ( 2 ), was designed and synthesized to investigate the influence of L ‐Leu to D ‐Leu residue replacement on the helical secondary structure of L ‐Leu‐Aib‐based dodecapeptides. Its preferred conformation was analyzed based on its Fourier transform infrared spectra, CD spectra, and X‐ray diffraction. It was revealed that peptide 2 formed a mixture of right‐handed ( P ) 3 10 ‐ and α‐helical structures in solution, and eight helical molecules were assembled in the crystalline state.
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Demizu et al. (2016) studied this question.
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