Abstract
Peptides are very flexible molecules, in contrast to proteins, which are stabilized by disulfide bridges and salt bridges in their tertiary structure. Peptides can adopt several conformations, at least in aqueous solutions. Some limitations, however, are imposed caused by then primary sequence. Two torsion angles characterize the free rotation of each peptide unit: the rotation about the Cα-CO-bond is called ψ-angle, the rotation about the Cα-NH-bond the φ-angle (Fig. 1 [1]). The torsion angle of the peptide bond, CO-NH, is about 180° and almost fixed owing to its double-bond character. Only certain combinations of ψ- and φ-angles are possible because of the steric hindering of carbonyl oxygen, amide hydrogen, and side-chain atoms of the amino acids.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Fasman, G. D. (1989) Prediction of protein structure and the principles of protein conformation. Plenum, New York.
Fauchere, J.-L. (1986) Elements for the rational design of peptide drugs. Adv. Drug Res. 15, 29–69.
Hruby, V. (1992) Strategies in the development of peptide antagonists. Progr. Brain Res. 92, 215–224.
Rizo, L. and Gierasch, L. (1992) Constrained peptides: models of bioactive peptides and their protein structures. Annu. Rev. Biochem. 61, 387–418.
Toniolo, C. (1990) Conformationally restrained peptides through short range cyclisation. Int. J. Pept. Protein Res. 35, 287–299.
Fields, G. and Noble, R. L. (1990) Solid phase peptide synthesis utilizing 9-fluor-enylmethoxycarbonyl amino acids. Int J. Pept Protein Res. 35, 161–214.
Atherton, E. and Sheppard, R. C. (1989) Solid Phase Peptide Synthesis: A Practical Approach. IRL, Oxford, UK.
Jung, G. and Beck-Sickinger, A. G. (1992) Multiple peptide synthesis. Angew Chem. Int. Ed. Engl. 31, 367–383.
Akaji, K., Tatsumi, T., Yoshida, M., Kimura, T., Fuiwara, Y., and Kiso, Y. (1992) Disulfide bond formation using the silyl chloride-sulfoxide system for the synthesis of cystine peptide. J. Am. Chem. Soc. 114, 4137–4143.
Gilon, C., Halle, D., Chorev, M., Selinger, Z., and Byk, G. (1991) Backbone cyclization: A new method for conferring conformational constraint on peptides. Biopolymers 31, 745–750.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Humana Press Inc. Totowa, NJ
About this protocol
Cite this protocol
Beck-Sickinger, A.G. (1997). Synthesis of Conformationally Restricted Peptides. In: Irvine, G.B., Williams, C.H. (eds) Neuropeptide Protocols. Methods in Molecular Biology™, vol 73. Humana Press. https://doi.org/10.1385/0-89603-399-6:61
Download citation
DOI: https://doi.org/10.1385/0-89603-399-6:61
Publisher Name: Humana Press
Print ISBN: 978-0-89603-399-3
Online ISBN: 978-1-59259-559-4
eBook Packages: Springer Protocols