Note added in proof. The bioactive peptides from milk have been reviewed recently [Teschemacher, H., Koch, G. & Brantl, v. (1997) Milk protein-derived opioid receptor ligands, Biopolym. Pept. Sci. 43, 99–117; Meisel, H. (1997) Biochemical properties of regulatory peptides derived from milk proteins, Biopolym. Pept. Sci. 43, 119–128]. The bifurcated hydrogen bonds in two intermediate 310/α helices have been described recently [Datta, S., Shamala, N., Banerjee, A. & Balaram, P. (1997) Hydrogen bonds in peptide helices. Analysis of two independent helices in the crystal stnictures of a peptide Boc-Val-Ala-Leu-Aib-Val-Ala-Phe-OMe, J. Pept. Res 49, 604–611].
Two-Dimensional 1H-NMR and CD Structural Analysis in a Micellar Medium of a Bovine αs1-Casein Fragment having Benzodiazepine-Like Properties
Article first published online: 16 JUL 2004
European Journal of Biochemistry
Volume 248, Issue 3, pages 872–878, September 1997
How to Cite
Lecouvey, M., Frochot, C., Miclo, L., Orlewski, P., Driou, A., Linden, G., Gaillard, J.-L., Marraud, M., Cung, M. T. and Vanderesse, R. (1997), Two-Dimensional 1H-NMR and CD Structural Analysis in a Micellar Medium of a Bovine αs1-Casein Fragment having Benzodiazepine-Like Properties. European Journal of Biochemistry, 248: 872–878. doi: 10.1111/j.1432-1033.1997.00872.x
- Issue published online: 16 JUL 2004
- Article first published online: 16 JUL 2004
- (Received 25 April/18 July 1997) – EJB 97 0595/3
- benzodiazepine-like peptide;
- molecular dynamics;
- circular dichroism
The conformation of the benzodiazepine-like decapeptide, YLGYLEQLLR, corresponding to residues 91–100 of bovine αs1-casein, has been examined in SDS micelles using CD, two-dimensional 1H-NMR and restrained molecular-dynamics simulation. Evidence is presented that the decapeptide adopts a rigid structure in water/SDS micellar medium, but not in water or dimethylsulfoxide. The three-dimensional structure, consistent with the proton-proton distances obtained from the quantitative analysis of the two-dimensional NOES, was generated by restrained energy minimization and molecular-dynamics simulation. In water/SDS micellar medium, YLCYLEQLLR adopts an amphipathic helicoid structure with distinct hydrophobic and hydrophilic faces. The relative disposition of the tyrosine aromatic rings was compared with that of the aromatic rings in the benzodiazepines.