|Title||Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the RF HIV-1 strain in water and water/trifluoroethanol solutions.|
|Publication Type||Journal Article|
|Year of Publication||1996|
|Authors||Vranken, W. F., M. Budesinsky, J. C. Martins, F. Fant, K. Boulez, H. Gras-Masse, and F. A. Borremans|
|Journal||Eur J Biochem|
|Date Published||1996 Feb 15|
|Keywords||Amino Acid Sequence, Circular Dichroism, HIV Envelope Protein gp120, HIV-1, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Peptides, Cyclic, Protein Conformation, Solutions, Trifluoroethanol, Water|
The disulfide-bridge-closed cyclic peptide corresponding to the whole V3 loop of the RF HIV-1 strain was examined by proton two-dimensional NMR spectroscopy in water and water/trifluoroethanol solutions. Although most of the peptide is conformationally averaged in water, the NOE data support a beta-turn conformation for the central conservative GPGR region and the presence of nascent helix. Upon addition of trifluoroethanol, helix formation in the C-terminal part becomes apparent. This is confirmed by CD data. NOEs indicative of multiple and transient beta-turns around the Asn6 glycosylation site and NOEs fitting X-ray data on a linear V3 peptide-Fab complex also emerge. The C-terminal helix is shown to have amphipathic character and might thus assist in the infection process.
|Alternate Journal||Eur. J. Biochem.|
Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the RF HIV-1 strain in water and water/trifluoroethanol solutions.