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. 2015 Apr 27;10(4):e0124839. doi: 10.1371/journal.pone.0124839

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)