Table 1. Hemoglobin-α subunit derived peptides interaction with gp120.
Peptides | Amino acid residues | Peptides sequence | Amino acid change | Anti-HIV activity | Charge | Hydrophobicity |
---|---|---|---|---|---|---|
Peptide- 1 | 25 | AHKLRVDPVNFKLLSHCLLVTLAAH (88–112) | _ | + | +2 | 56% |
Analogue of peptide-1 (1a) | 25 | AHKLRVDPVNFKLLSHCLLVTLARH (88–112) | (A24R) | + | +3 | 52% |
Analogue of peptide-1 (1b) | 25 | AHKLRVDPVNCKLLSHCLLVTLARH (88–112) | (F11C) and (A24R) | ++ | +3 | 52% |
Peptide- 2 | 29 | SAQVKGHGKKVADALTNAVAHVDDMPNAL (52–80) | _ | NA | 0 | 44% |
Peptide- 3 | 29 | VKGHGKKVADALTNAVAHVDDMPNALSAL (55–83) | _ | + | 0 | 48% |
Analogue of peptide-3 | 29 | VKGHRKKVADALRRAVAHVDDMPRALSAL (55–83) | (G5R, N13R, A14R & N24R) | NA | +4 | 48% |
Scrambled peptide(sP) | 25 | PLVKDVLRSLCNHAHKCVTLALLRH (for peptide-1) (88–112) | _ | NA | +3 | 52% |
Sequences of the designed peptides along with analogues are enlisted in the table. Amino acids indicated in bold-underlined are the changes made in the sequence of peptide-1 and peptide-3 to design their analogues. The regions of human Hb-α from which sequence of amino acids of these peptides was taken, is given in the parenthesis. (+: moderate, ++: significant, NA: No activity)