Effects of cathelicidin and its fragments on three key enzymes of HIV-1
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AbstractCathelicidins 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 15 mu M, 7 mu M, and 70 mu M respectively. The three peptides inhibited HIV-1 protease with a weak potency, achieving 20-30% inhibition at 100 mu M. 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. (C) 2011 Elsevier Inc. All rights reserved.
All Author(s) ListWong JH, Legowska A, Rolka K, Ng TB, Hui M, Cho CH, Lam WWL, Au SWN, Gu OW, Wan DCC
Journal namePeptides
Detailed descriptionTo ORKTS: DOI: 10.1016/j.peptides.2011.04.017
Year2011
Month6
Day1
Volume Number32
Issue Number6
PublisherElsevier
Pages1117 - 1122
ISSN0196-9781
eISSN1873-5169
LanguagesEnglish-United Kingdom
KeywordsCathelicidin; Fragments; HIV reverse transcriptase; Integrase; Protease
Web of Science Subject CategoriesBiochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY; Pharmacology & Pharmacy; PHARMACOLOGY & PHARMACY

Last updated on 2020-26-11 at 00:38