Publication: Trishomocubane amino acid as a β-turn scaffold
Issued Date
2008-02-01
Resource Type
ISSN
17470277
Other identifier(s)
2-s2.0-38549132812
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Mahidol University
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SCOPUS
Bibliographic Citation
Chemical Biology and Drug Design. Vol.71, No.2 (2008), 125-130
Suggested Citation
Fernando Albericio, Per I. Arvidson, Krishna Bisetty, Ernest Giralt, Thavendran Govender, Samuel Jali, Palangpon Kongsaeree, Hendrik G. Kruger, Samran Prabpai Trishomocubane amino acid as a β-turn scaffold. Chemical Biology and Drug Design. Vol.71, No.2 (2008), 125-130. doi:10.1111/j.1747-0285.2007.00618.x Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/18979
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Title
Trishomocubane amino acid as a β-turn scaffold
Abstract
The synthesis and X-ray structure of two diasteriomeric heptapeptides [Ac-Ala-Ala-Ala-(R/S)-Cage-Ala-Ala-Ala-NH2] 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 310-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. © 2008 The Authors.