CD and nmr characterizations are reported for the 23-mer peptide CMC;I, corresponding to residues 577-599 of gp41, the transmembrane glycoplotein of the human immunodeficiency virus I. Concentration, temperature, and pH dependencies of CD and nmr spectra are indicative of self-association with a consequent stabilization of secondary structural elements in water. The addition to the water solution of small amounts of trifluoroethanol induces a secondary structure, mostly due to the presence of helical elements. The amphipathic character of the helix and the presence of three hydrophobic 4/3 heptad repeats suggest that the peptide could be structured in a symmetric association of helices, such as in a coiled-coil structure. This behavior is discussed in terms of a possible role of this segment in the gp41 envelope oligomerization.

NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41

Consonni R;Ragona L;Zetta L
1996

Abstract

CD and nmr characterizations are reported for the 23-mer peptide CMC;I, corresponding to residues 577-599 of gp41, the transmembrane glycoplotein of the human immunodeficiency virus I. Concentration, temperature, and pH dependencies of CD and nmr spectra are indicative of self-association with a consequent stabilization of secondary structural elements in water. The addition to the water solution of small amounts of trifluoroethanol induces a secondary structure, mostly due to the presence of helical elements. The amphipathic character of the helix and the presence of three hydrophobic 4/3 heptad repeats suggest that the peptide could be structured in a symmetric association of helices, such as in a coiled-coil structure. This behavior is discussed in terms of a possible role of this segment in the gp41 envelope oligomerization.
1996
Istituto per lo Studio delle Macromolecole - ISMAC - Sede Milano
HELICAL COILED-COILS
ENVELOPE GLYCOPROTEIN
LEUCINE ZIPPER
PHOTO-CIDNP
AMINO-ACIDS
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/178905
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