Structural studies on synthetic peptides from the principal neutralizing domain of HIV-1 gp120 that bind to CD4 and enhance HIV-1 infection.
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.
Dettin
M
M
Institute of Industrial Chemistry, University of Padua, Italy.
De Rossi
A
A
Autiero
M
M
Guardiola
J
J
Chieco-Bianchi
L
L
Di Bello
C
C
D000595:Amino Acid Sequence; D015704:CD4 Antigens / Q000378:metabolism*; D002942:Circular Dichroism; D005583:Fourier Analysis; D015699:HIV Envelope Protein gp120 / Q000737:chemistry / Q000378:metabolism*; D015497:HIV-1 / Q000378:metabolism* / Q000502:physiology; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; D010446:Peptide Fragments