Home | My Profile | Contact Us
Research Trends Products  |   order gateway  |   author gateway  |   editor gateway  
Register | Forgot Password

Author Resources
 Author Gateway
 Article submission guidelines

Editor Resources
 Editor/Referee Gateway

 Regional Subscription Agents/Distributors
Current Topics in Peptide & Protein Research   Volumes    Volume 1  Issue 1
The use of synthetic peptides in the study of HIV-1/target cell interactions
Carlo Di Bello, Monica Dettin, Luigi Chieco-Bianchi, Anita De Rossi, John Guardiola, Monica Autiero
Pages: 65 - 73
Number of pages: 9
Current Topics in Peptide & Protein Research
Volume 1  Issue 1

Copyright © 1994 Research Trends. All rights reserved

Synthetic peptides spanning specific sequences of HIV-1 gp120 principal neutralizing domain, and T-lymphocyte CD4 were characterized and utilized to study the complex interactions between these two important proteins, at the molecular level. CD4 interactions with gp120 and gp120-derived peptides were studied using an in vitro assay based on immobilized recombinant soluble CD4. In this system, CD4 binds to peptides corresponding to the principal neutralizing domain of the envelope protein. Competition experiments indicated that our principal neutralizing domain-related synthetic peptides were specifically recognized by a CD4 site adjacent to, but distinct from, the high affinity gp120-binding site of CD4. Interestingly, we also found that a peptide designed from the principal neutralizing domain of HIV-1 MN virus greatly enhanced viral infection: the observed effect occurred in the early steps of viral infection and was not strain-restricted. The biological assays performed on point-mutated and/or shortened analogues of the active peptide, in addition to conformational spectroscopic measurements and theoretical calculations, allowed the formulation of a model that was utilized to interpret the experimental data. Two CD4-derived peptides, corresponding to residues 37-53 and 37-55 of the V1 domain of CD4, which were recently proposed as the most likely binding site of HIV-1 gp120 on CD4, were also synthesized chemically by solid-phase techniques. Their ability to inhibit the infectivity of different HIV-1 strains in different cell lines was monitored by several biological assays and by electron microscopy. Preliminary findings suggest that the peptides inhibit HIV-1 infectivity only slightly, without any detectable cytotoxicity.
Buy this Article


Buy this article
Buy this volume
Subscribe to this title
Shopping Cart

Quick Links
Search Products
Browse in Alphabetical Order : Journals
Browse by Subject Classification : Journals

Ordering Information Ordering Information
Downloadable forms Downloadable Forms