The design of a specific ligand of HIV gp120.
The crystal structure of CD4 suggested that the C/G38 and C/L44 replacements with the consequent cystine bridge formation are compatible with the native structure of that molecular moiety. As the NQGSF sequence, corresponding to the 39-43 fragment of human CD4 protein, was found to be involved in the HIV gp120 interaction, it has been synthesized in a cyclic form by adding two cysteine residues at the amino and carboxy termini. 1H-NMR studies show that the predominant solution conformation of cyclo-[CNQGSFC] is a type II beta-turn centred on the NQGS segment. Structural and dynamic properties of the peptide are also analysed in relation to the in vitro activity.
Scarselli
M
M
Dipartimento di Biologia Molecolare, Università di Siena, Italy.
Facchiano
A
A
Russo
G
G
Molinari
H
H
Ragona
L
L
Zetta
L
L
Niccolai
N
N
D000595:Amino Acid Sequence; D015704:CD4 Antigens / Q000737:chemistry* / Q000378:metabolism; D015726:Giant Cells / Q000187:drug effects / Q000821:virology; D015699:HIV Envelope Protein gp120 / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides / Q000737:chemistry* / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000494:pharmacology; D011487:Protein Conformation
D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; D008024:Ligands; D009842:Oligopeptides; D010456:Peptides, Cyclic