Trishomocubane amino acid as a β-turn scaffold
2008 (English)In: Chemical biology & drug design, ISSN 1747-0277, Vol. 71, no 2, 125-130 p.Article in journal (Refereed) Published
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 beta-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 beta-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 m-helix classification. These experimental results confirm previous theoretical studies in our laboratory which predicted that the cage moiety would be a strong/active beta-turn inducer.
Place, publisher, year, edition, pages
Wiley , 2008. Vol. 71, no 2, 125-130 p.
AMBER, beta-turn, cage peptide, trishomocubane amino acid, X-ray structure
IdentifiersURN: urn:nbn:se:uu:diva-112408DOI: 10.1111/j.1747-0285.2007.00618.xISI: 000253456500004OAI: oai:DiVA.org:uu-112408DiVA: diva2:286166