1. Effects of cathelicidin and its fragments on three key enzymes of HIV-1
- Author
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Wong, Jack Ho, Legowska, Anna, Rolka, Krzysztof, Ng, Tzi Bun, Hui, Mamie, Cho, Chi Hin, Lam, Wendy Wai Ling, Au, Shannon Wing Ngor, Gu, Oscar Wangang., and Wan, David Chi Cheong
- Subjects
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PEPTIDE antibiotics , *HIV , *LIFE cycles (Biology) , *PROTEOLYTIC enzymes , *PROTEIN-protein interactions , *REVERSE transcriptase inhibitors , *SURFACE plasmon resonance , *GREEN fluorescent protein - Abstract
Abstract: Cathelicidins exhibit anti-HIV activity but it is not known if they reduce the activity of enzymes crucial to the life cycle of the retrovirus. It is shown in this investigation that human cathelicidin LL37 and its fragments LL13-37 and LL17-32 inhibited HIV-1 reverse transcriptase dose-dependently with an IC50 value of 15μM, 7μM, and 70μM, respectively. The three peptides inhibited HIV-1 protease with a weak potency, achieving 20–30% inhibition at 100μM. The mechanism of inhibition was protein–protein interaction as revealed by surface plasmon resonance. The peptides were devoid of the ability to inhibit translocation of HIV-1 integrase, which has been labeled with green fluorescent protein, into the nucleus. The peptides did not exert toxicity on human peripheral blood mononuclear cells. [Copyright &y& Elsevier]
- Published
- 2011
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