SrasV1, PubMed, Checkpoint, bibRecord, 001387

Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7.

Identifieur interne : 001387 ( PubMed/Checkpoint ); précédent : 001386; suivant : 001388

Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7.

Auteurs : Yaoqing Chen [République populaire de Chine] ; Luyang Cao ; Maohua Zhong ; Yan Zhang ; Chen Han ; Qiaoli Li ; Jingyi Yang ; Dihan Zhou ; Wei Shi ; Benxia He ; Fang Liu ; Jie Yu ; Ying Sun ; Yuan Cao ; Yaoming Li ; Wenxin Li ; Deying Guo ; Zhijian Cao ; Huimin Yan

Source :

PloS one [ 1932-6203 ] ; 2012.

RBID : pubmed:22536342

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Anti-HIV Agents (chemical synthesis), Anti-HIV Agents (pharmacology), Anti-HIV Agents (toxicity), Antimicrobial Cationic Peptides (chemical synthesis), Antimicrobial Cationic Peptides (pharmacology), Antimicrobial Cationic Peptides (toxicity), Cell Line, Dose-Response Relationship, Drug, Drug Design, HIV-1 (drug effects), Humans, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary, Scorpion Venoms (chemical synthesis), Scorpion Venoms (pharmacology), Scorpion Venoms (toxicity).
MESH :
- chemical , chemical synthesis : Anti-HIV Agents, Antimicrobial Cationic Peptides, Scorpion Venoms.
- chemical , pharmacology : Anti-HIV Agents, Antimicrobial Cationic Peptides, Scorpion Venoms.
- chemical , toxicity : Anti-HIV Agents, Antimicrobial Cationic Peptides, Scorpion Venoms.
- drug effects : HIV-1.
- Amino Acid Sequence, Cell Line, Dose-Response Relationship, Drug, Drug Design, Humans, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary.

Abstract

For over 30 years, HIV/AIDS has wreaked havoc in the world. In the absence of an effective vaccine for HIV, development of new anti-HIV agents is urgently needed. We previously identified the antiviral activities of the scorpion-venom-peptide-derived mucroporin-M1 for three RNA viruses (measles viruses, SARS-CoV, and H5N1). In this investigation, a panel of scorpion venom peptides and their derivatives were designed and chosen for assessment of their anti-HIV activities. A new scorpion venom peptide derivative Kn2-7 was identified as the most potent anti-HIV-1 peptide by screening assays with an EC(50) value of 2.76 µg/ml (1.65 µM) and showed low cytotoxicity to host cells with a selective index (SI) of 13.93. Kn2-7 could inhibit all members of a standard reference panel of HIV-1 subtype B pseudotyped virus (PV) with CCR5-tropic and CXCR4-tropic NL4-3 PV strain. Furthermore, it also inhibited a CXCR4-tropic replication-competent strain of HIV-1 subtype B virus. Binding assay of Kn2-7 to HIV-1 PV by Octet Red system suggested the anti-HIV-1 activity was correlated with a direct interaction between Kn2-7 and HIV-1 envelope. These results demonstrated that peptide Kn2-7 could inhibit HIV-1 by direct interaction with viral particle and may become a promising candidate compound for further development of microbicide against HIV-1.

DOI: 10.1371/journal.pone.0034947
PubMed: 22536342

Affiliations:

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001373
to stream PubMed, to step Curation: 001373

Links to Exploration step

pubmed:22536342

Le document en format XML

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<front><div type="abstract" xml:lang="en">For over 30 years, HIV/AIDS has wreaked havoc in the world. In the absence of an effective vaccine for HIV, development of new anti-HIV agents is urgently needed. We previously identified the antiviral activities of the scorpion-venom-peptide-derived mucroporin-M1 for three RNA viruses (measles viruses, SARS-CoV, and H5N1). In this investigation, a panel of scorpion venom peptides and their derivatives were designed and chosen for assessment of their anti-HIV activities. A new scorpion venom peptide derivative Kn2-7 was identified as the most potent anti-HIV-1 peptide by screening assays with an EC(50) value of 2.76 µg/ml (1.65 µM) and showed low cytotoxicity to host cells with a selective index (SI) of 13.93. Kn2-7 could inhibit all members of a standard reference panel of HIV-1 subtype B pseudotyped virus (PV) with CCR5-tropic and CXCR4-tropic NL4-3 PV strain. Furthermore, it also inhibited a CXCR4-tropic replication-competent strain of HIV-1 subtype B virus. Binding assay of Kn2-7 to HIV-1 PV by Octet Red system suggested the anti-HIV-1 activity was correlated with a direct interaction between Kn2-7 and HIV-1 envelope. These results demonstrated that peptide Kn2-7 could inhibit HIV-1 by direct interaction with viral particle and may become a promising candidate compound for further development of microbicide against HIV-1.</div>
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<Abstract><AbstractText>For over 30 years, HIV/AIDS has wreaked havoc in the world. In the absence of an effective vaccine for HIV, development of new anti-HIV agents is urgently needed. We previously identified the antiviral activities of the scorpion-venom-peptide-derived mucroporin-M1 for three RNA viruses (measles viruses, SARS-CoV, and H5N1). In this investigation, a panel of scorpion venom peptides and their derivatives were designed and chosen for assessment of their anti-HIV activities. A new scorpion venom peptide derivative Kn2-7 was identified as the most potent anti-HIV-1 peptide by screening assays with an EC(50) value of 2.76 µg/ml (1.65 µM) and showed low cytotoxicity to host cells with a selective index (SI) of 13.93. Kn2-7 could inhibit all members of a standard reference panel of HIV-1 subtype B pseudotyped virus (PV) with CCR5-tropic and CXCR4-tropic NL4-3 PV strain. Furthermore, it also inhibited a CXCR4-tropic replication-competent strain of HIV-1 subtype B virus. Binding assay of Kn2-7 to HIV-1 PV by Octet Red system suggested the anti-HIV-1 activity was correlated with a direct interaction between Kn2-7 and HIV-1 envelope. These results demonstrated that peptide Kn2-7 could inhibit HIV-1 by direct interaction with viral particle and may become a promising candidate compound for further development of microbicide against HIV-1.</AbstractText>
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Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7.

Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7.

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