T22 peptide, also known as [Tyr5,12,Lys7]-polyphemusin II peptide, is a short, positively charged peptide, analog of polyphemusin peptide which exerts a strong anti- HIV activity. Polyphemusins are known to inhibit the growth of gram-negative bacteria and some fungi such as Candida Albicans. T22peptide is a potent antagonist of CXCR4 (IC50 = 5.05 nM), a co-receptor used by HIV to penetrate cells. It has been suggested that [Tyr5,12,Lys7]-polyphemusin II peptide exerts its effect against HIV-1 especially by blocking virus-cell fusion and that T22 might interact with HIV envelope protein (such as gp120 ) and T-cell surface protein. T22peptide antiviral activity has been shown on HIV-infected MT-4 cells with an IC50 of 0.008 µg/mL (2.6 nM). The cytotoxic concentration on HIV virus (CC50) of T22 is 54 µg/mL (17 mM).
Delivery format : Freeze dried in propylene 2mL microtubes
Other names : T22 Protein ; Tyr(5,12),Lys(7))-polyphemusin II peptide ; 5,12-Tyr-7-Lys-polyphemusin II ; 5,12-tyrosyl-7-lysylpolyphemusin II ; L000589 ; 142960-16-5
The [Tyr5,12,Lys7]-polyphemusin II peptide (T22) inhibits HIV-1 replication in lymphocytes. The mechanism of T22 inhibition of HIV-1 replication may involve T22 competition with HIV-1 for attachment sites on the plasma membrane of targeted cells. Here we find that the T22 peptide binds to the CD4 molecule in affinity columns. We also find that antiserum to CD4 inhibits cell attachment to T22. Further CD4+ transfected cells attach to T22 while their parental cells which do not express CD4 do not attach to T22. These data demonstrate that T22 binds to the CD4 molecule and supports the hypothesis that T22 inhibits HIV-1 replication by binding to the cell surface CD4 molecule and inhibiting uptake of the virus.
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