A study of effects of peptide fragments of bovine and human lactoferrins on activities of three key HIV-1 enzymes

• Human lactoferricin was potent in inhibiting HIV-1 reverse transcriptase (IC50 = 2 μM).
• Human lactoferrampin and bovine lactoferrampin showed obvious inhibitory effect on HIV-1 integrase at 37 μM and 18.5 μM, respectively.
• Human and bovine lactoferrin fragments showed only a slight inhibitory effect (from slightly below 2% to 6% inhibition) on HIV-1 protease.

The intent of this study was to examine human and bovine lactoferrin fragments including lactoferrin (1-11), lactoferricin and lactoferrampin, all of which did not demonstrate hemolytic activity toward rabbit erythrocytes at 1 mM concentration, for possible inhibitory effects on the activities of HIV-1 reverse transcriptase, protease and integrase. The data showed that human lactoferricin was the most potent in inhibiting HIV-1 reverse transcriptase (IC50 =2 μM). Bovine lactoferricin (IC50 = 10 μM) and bovine lactoferrampin (IC50 = 150 μM) were less potent. Human lactoferrampin and human and bovine lactoferrin (1-11) at 1 mM concentration did not exhibit any inhibitory effect on HIV-1 reverse transcriptase. All peptides showed only a slight inhibitory effect (from slightly below 2% to 6% inhibition) on HIV-1 protease. Human lactoferrampin and bovine lactoferrampin showed obvious inhibitory effect on HIV-1 integrase at 37 μM and 18.5 μM, respectively. The HIV-1 integrase inhibitory activity of human lactoferrampin and bovine lactoferrampin was dose-dependent. The other peptides were devoid of HIV-1 integrase inhibitory activity. Thus, it is concluded that some lactoferrin fragments exert an inhibitory action on HIV-1 reverse transcriptase and HIV-1 integrase.