ArticlePloS one2015
New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Advances in Discovery and Design of Anti-influenza Virus Peptides.Current medicinal chemistry · 2026Review
- Research strategies of the N-peptide fusion inhibitor: a promising direction for discovering novel antivirals.Journal of virology · 2025Review
- Antiviral strategies against influenza virus: an update on approved and innovative therapeutic approaches.Cellular and molecular life sciences : CMLS · 2025Review
- SARS-CoV-2 Fusion Peptide Conjugated to a Tetravalent Dendrimer Selectively Inhibits Viral Infection.Pharmaceutics · 2023Article
- Production and characterization of lentivirus vector-based SARS-CoV-2 pseudoviruses with dual reporters: Evaluation of anti-SARS-CoV-2 viral effect of Korean Red Ginseng.Journal of ginseng research · 2023Article
- Antiviral Peptides as Anti-Influenza Agents.International journal of molecular sciences · 2022Review
- Antimicrobial peptides and their potential application in antiviral coating agents.Colloids and surfaces. B, Biointerfaces · 2022Review
- Influenza Virus Entry inhibitors.Advances in experimental medicine and biology · 2022Review
- Viral Prefusion Targeting Using Entry Inhibitor Peptides: The Case of SARS-CoV-2 and Influenza A virus.International journal of peptide research and therapeutics · 2022Article
- Advances in the development of entry inhibitors for sialic-acid-targeting viruses.Drug discovery today · 2021Review
- The seafood Musculus senhousei shows anti-influenza A virus activity by targeting virion envelope lipids.Biochemical pharmacology · 2020Article
- Anti-Influenza Treatment: Drugs Currently Used and Under Development.Archivos de bronconeumologia · 2017Review
- A "building block" approach to the new influenza A virus entry inhibitors with reduced cellular toxicities.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A viral (IAV) fusion peptides are known for their important role in viral-cell fusion process and membrane destabilization potential which are compatible with those of antimicrobial peptides. Thus, by replacing the negatively or neutrally charged residues of FPs with positively charged lysines, we synthesized several potent antimicrobial peptides derived from the fusogenic peptides (FPs) of hemagglutinin glycoproteins (HAs) of IAV. The biological screening identified that in addition to the potent antibacterial activities, these positively charged fusion peptides (pFPs) effectively inhibited the replication of influenza A viruses including oseltamivir-resistant strain. By employing pseudovirus-based entry inhibition assays including H5N1 influenza A virus (IAV), and VSV-G, the mechanism study indicated that the antiviral activity may be associated with the interactions between the HA2 subunit and pFP, of which, the nascent pFP exerted a strong effect to interrupt the conformational changes of HA2, thereby blocking the entry of viruses into host cells. In addition to providing new peptide "entry blockers", these data also demonstrate a useful strategy in designing potent antibacterial agents, as well as effective viral entry inhibitors. It would be meaningful in treatment of bacterial co-infection during influenza pandemic periods, as well as in our current war against those emerging pathogenic microorganisms such as IAV and HIV.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.