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.

TitleConformational 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 TypeJournal Article
Year of Publication1996
AuthorsVranken, W. F., M. Budesinsky, J. C. Martins, F. Fant, K. Boulez, H. Gras-Masse, and F. A. Borremans
JournalEur J Biochem
Volume236
Issue1
Pagination100-8
Date Published1996 Feb 15
ISSN0014-2956
KeywordsAmino 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
Abstract

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 JournalEur. J. Biochem.
PubMed ID8617252
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