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- W2040217773 abstract "The synthesis and X‐ray structure of two diasteriomeric heptapeptides [Ac‐Ala‐Ala‐Ala‐( R/S )‐Cage‐Ala‐Ala‐Ala‐NH 2 ] with a trishomocubane amino acid as a β‐turn scaffold are reported. The amino acid was synthesized as a racemate and two diastereomeric peptides were obtained. The two peptides were separated by preparative high‐pressure liquid chromatography and crystals suitable for X‐ray analysis were grown for both diasteriomeric peptides. In general, both the peptides satisfy the criteria for β‐turn conformations. Five of the six Ala residues of both cage peptide crystals satisfy the criteria for 3 10 ‐helix characteristics and the cage amino acid residue satisfied the α‐helix classification. These experimental results confirm previous theoretical studies in our laboratory which predicted that the cage moiety would be a strong/active β‐turn inducer." @default.
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- W2040217773 date "2008-01-17" @default.
- W2040217773 modified "2023-10-16" @default.
- W2040217773 title "Trishomocubane Amino Acid as a β-turn scaffold" @default.
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- W2040217773 doi "https://doi.org/10.1111/j.1747-0285.2007.00618.x" @default.
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