Investigations Using Photo Affinity Labeled Analogues Confirm the Binding between sCD4 and the PND of HIV-1, MN

In previous studies we demonstrated that a synthetic peptide corresponding to the sequence in the (307-330) region of the gp120 principal neutralizing domain of the HIV-1 MN strain is able to bind sCD4 in an affinity chromatography assay and to enhance CD4 expression, CD4 affinity for gp120, and HIV...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-12, Vol.241 (2), p.584-588
Main Authors: Dettin, Monica, Scarinci, Claudia, Seraglia, Roberta, Bello, Carlo Di
Format: Article
Language:English
Subjects:
AIDS/HIV
Binding Sites
CD4 Antigens - metabolism
HIV Envelope Protein gp120 - metabolism
HIV-1 - classification
HIV-1 - metabolism
Peptide Fragments - metabolism
Photoaffinity Labels
Protein Binding
Solubility
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In previous studies we demonstrated that a synthetic peptide corresponding to the sequence in the (307-330) region of the gp120 principal neutralizing domain of the HIV-1 MN strain is able to bind sCD4 in an affinity chromatography assay and to enhance CD4 expression, CD4 affinity for gp120, and HIV-1 infection. This paper describes a photo affinity labeling experiment, designed to confirm the gp120 peptide–CD4 interaction and to locate the binding site of the synthetic peptide on the CD4 molecule. To this end two specifically marked analogues of the peptide patterned on the (307-330) region of HIV-MN-gp120, in which the Tyr1residue is replaced with Phe(p-N3) or Phe(p-NO2), have been synthesized. Irradiation of CD4 solutions in the presence of both analogues produced a new component, the mass value of which confirms the formation of a covalent bond between the peptide and the protein.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.7857