ArticleScientific reports2016
A "building block" approach to the new influenza A virus entry inhibitors with reduced cellular toxicities.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Structure-Guided Design of Peptide Inhibitors Targeting Class I Viral Fusion Proteins.Pathogens (Basel, Switzerland) · 2025Review
- A Comprehensive Overview of Antimicrobial Peptides: Broad-Spectrum Activity, Computational Approaches, and Applications.Antibiotics (Basel, Switzerland) · 2025Review
- Antiviral Peptides as Anti-Influenza Agents.International journal of molecular sciences · 2022Review
- Biomechanical Features of Graphene-Augmented Inorganic Nanofibrous Scaffolds and Their Physical Interaction with Viruses.Materials (Basel, Switzerland) · 2020Article
- The seafood Musculus senhousei shows anti-influenza A virus activity by targeting virion envelope lipids.Biochemical pharmacology · 2020Article
- The inducible amphisome isolates viral hemagglutinin and defends against influenza A virus infection.Nature communications · 2020Article
- Anti-Influenza A Viral Butenolide fromViruses · 2018Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A virus (IAV) is a severe worldwide threat to public health and economic development that results in the emergence of drug-resistant or highly virulent strains. Therefore, it is imperative to develop potent anti-IAV drugs with different modes of action to currently available drugs. Herein, we show a new class of antiviral peptides generated by conjugating two known short antiviral peptides: part-1 (named Jp with the sequence of ARLPR) and part-2 (named Hp with the sequence of KKWK). The new peptides were thus created by hybridization of these two domains at C- and N- termini, respectively. The anti-IAV screening results identified that C20-Jp-Hp was the most potent peptide with IC50 value of 0.53 μM against A/Puerto Rico/8/34 (H1N1) strain. Interestingly, these new peptides display lower toxicities toward mammalian cells and higher therapeutic indices than their prototypes. In addition, the mechanism of action of C20-Jp-Hp was extensively investigated.
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