Structural studies on synthetic peptides from the principal neutralizing domain of HIV-1 GP120 that bind to CD4 and enhance HIV-1 infection

M. Dettin, A. De Rossi, M. Autiero, J. Guardiola, L. Chieco-Bianchi, C. Di Bello

Research output: Contribution to journalArticlepeer-review

Abstract

In previous studies we have demonstrated that synthetic peptides, corresponding to sequences in the (307-330) region of the gp120 principal neutralizing domain of different HIV-1 isolates are specifically recognized by a site distinct from the high affinity gp120-binding site of CD4. Interestingly, a peptide designed from the HIV-1 MN strain is able to enhance viral infection, while a HTLV-IIIB derived analogue is at least ten-fold less efficient and no effect is shown by other tested peptides. This enhancing effect occurs in the early step of infection and it is not strain restricted. A correlation between structure and biological functions evidenced by CD, FT- IR, and preliminary mono and bidimensional NMR is presented in this paper. The experimental data are compared to the predictions obtained by theoretical calculations.

Original languageEnglish
Pages (from-to)364-370
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume191
Issue number2
DOIs
Publication statusPublished - 1993

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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