Biological and conformational studies on analogues of a synthetic peptide enhancing HIV-1 infection.
We have previously demonstrated that a 23-amino acid peptide derived from the V3 loop of the surface glycoprotein of the HIV-1 strain MN is able to bind CD4 and to enhance HIV-1 infection. Further studies have suggested that the peptide/CD4 interaction induces an increase in both CD4 expression and CD4/gp120 binding affinity. This paper describes the biological and physico-chemical characterization of three analogues of reduced sequence that have been designed in order to identify the minimum active sequence of this peptide corresponding to the MN-HIV- 1 principal neutralizing domain. Biological studies indicate that the entire sequence is required for biological activity and that the sequence 1-18 presents an inhibitory activity. CD and FT-IR absorption data are discussed here in order to identify possible structure-function correlations.
Dettin
M
M
Department of Chemical Process Engineering, University of Padua, Italy. peptide@uxl.unipd.it
Scarinci
C
C
Zanotto
C
C
Roncon
R
R
De Rossi
A
A
Di Bello
C
C
D000595:Amino Acid Sequence; D002460:Cell Line / Q000821:virology; D002942:Circular Dichroism; D017124:Conserved Sequence; D004305:Dose-Response Relationship, Drug; D015699:HIV Envelope Protein gp120 / Q000737:chemistry*; D015497:HIV-1 / Q000472:pathogenicity*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000494:pharmacology*; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared; D013329:Structure-Activity Relationship
D015699:HIV Envelope Protein gp120; C059762:HIV envelope protein gp120 (305-321); D010446:Peptide Fragments