Fernando AlbericioPer I. ArvidsonKrishna BisettyErnest GiraltThavendran GovenderSamuel JaliPalangpon KongsaereeHendrik G. KrugerSamran PrabpaiUniversitat de BarcelonaUppsala UniversitetDurban University of TechnologyUniversity of KwaZulu-NatalMahidol University2018-07-122018-07-122008-02-01Chemical Biology and Drug Design. Vol.71, No.2 (2008), 125-130174702772-s2.0-38549132812https://repository.li.mahidol.ac.th/handle/20.500.14594/18979The 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1111/j.1747-0285.2007.00618.x