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 β-turn centred on the NQGS segment. Structural and dynamic properties of the peptide are also analysed in relation to the in vitro activity. © 1997 European Peptide Society and John Wiley & Sons, Ltd.
Scarselli, M., Facchiano, A., Russo, G., Molinari, H., Ragona, L., Zetta, L., et al. (1997). The design of a specific ligand of HIV gp120. JOURNAL OF PEPTIDE SCIENCE, 3(5), 383-390 [10.1002/(SICI)1099-1387(199709)3:5<383].
The design of a specific ligand of HIV gp120
Niccolai, N.
1997-01-01
Abstract
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 β-turn centred on the NQGS segment. Structural and dynamic properties of the peptide are also analysed in relation to the in vitro activity. © 1997 European Peptide Society and John Wiley & Sons, Ltd.
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https://hdl.handle.net/11365/35174
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