Abstract
Cyclic peptides are excellent models for reverse turns, and it is well established that the cyclic hexapeptides contain two β-turns. In our previous studies, we reported the conformation of cyclo(Pro-Leu-Gly)2, and also the influence of the two Cα methyl groups of Aib on the formation of β-turns and overall conformation of cyclo-(Pro-Leu-Aib)2 [1,2]. The structure of cyclo(Pro-Leu-Gly)2 was comprised of two type I β-turns and the molecule had an overall C2 symmetry. The cyclo(Pro-Leu-Aib)2, however, exhibited an asymmetrical conformation containing two different types of β-turn (type II′ and type VI).
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References
Wang, J., Osada, S., Kodama, H., Kato, T., Kondo, M. Bull. Chem. Soc. Jpn. 72, 533–540 (1999).
Wang, J., Osada, S., Kodama, T., Kondo, M. Bull Chem. Soc. Jpn. 73, 1221–1226 (2000).
Gierasch, L.M., Deber, C.M., Madison, V., Niu, C., Blout, E.R. Biochemistry 20, 4730–4738 (1981).
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© 2001 Springer Science+Business Media Dordrecht
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Osada, S. et al. (2001). Synthesis and Solution Structures of Cyclic Hexapeptides Cyclo(Pro-Leu-Xxx)2 . In: Lebl, M., Houghten, R.A. (eds) Peptides: The Wave of the Future. American Peptide Symposia, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0464-0_217
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DOI: https://doi.org/10.1007/978-94-010-0464-0_217
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