ArticlePloS one2013
Inhibition of influenza A virus infection in vitro by peptides designed in silico.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Nanobody peptide conjugate: a novel CD163 based broad neutralizing strategy against porcine reproductive and respiratory syndrome virus.Journal of nanobiotechnology · 2024Article
- Antiviral polysaccharide and antiviral peptide delivering nanomaterials for prevention and treatment of SARS-CoV-2 caused COVID-19 and other viral diseases.Journal of controlled release : official journal of the Controlled Release Society · 2023Review
- Antiviral Peptides as Anti-Influenza Agents.International journal of molecular sciences · 2022Review
- Neutralizing Effect of Synthetic Peptides toward SARS-CoV-2.ACS omega · 2022Article
- Review of antiviral peptides for use against zoonotic and selected non-zoonotic viruses.Peptides · 2021Review
- Nanoscale pathogens treated with nanomaterial-like peptides: a platform technology appropriate for future pandemics.Nanomedicine (London, England) · 2021Review
- Peptides to combat viral infectious diseases.Peptides · 2020Review
- Antiviral peptides as promising therapeutic drugs.Cellular and molecular life sciences : CMLS · 2019Review
- In-silico design and molecular docking evaluation of peptides derivatives from bacteriocins and porcine beta defensin-2 as inhibitors of Hepatitis E virus capsid protein.Virusdisease · 2017Article
- Evaluation of peptide designing strategy against subunit reassociation in mucin 1: A steered molecular dynamics approach.PloS one · 2017Article
- A "building block" approach to the new influenza A virus entry inhibitors with reduced cellular toxicities.Scientific reports · 2016Article
- Anti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus Binding.PloS one · 2016Article
- AVP-IC50 Pred: Multiple machine learning techniques-based prediction of peptide antiviral activity in terms of half maximal inhibitory concentration (IC50).Biopolymers · 2015Article
- Structure-based design of novel naproxen derivatives targeting monomeric nucleoprotein of Influenza A virus.Journal of biomolecular structure & dynamics · 2015Article
- The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems.Chemical Society reviews · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A viruses are enveloped, segmented negative single-stranded RNA viruses, capable of causing severe human respiratory infections. Currently, only two types of drugs are used to treat influenza A infections, the M2 H(+) ion channel blockers (amantadine and rimantadine) and the neuraminidase inhibitors (NAI) (oseltamivir and zanamivir). Moreover, the emergence of drug-resistant influenza A virus strains has emphasized the need to develop new antiviral agents to complement or replace the existing drugs. Influenza A virus has on the surface a glycoprotein named hemagglutinin (HA) which due to its important role in the initial stage of infection: receptor binding and fusion activities of viral and endosomal membranes, is a potential target for new antiviral drugs. In this work we designed nine peptides using several bioinformatics tools. These peptides were derived from the HA1 and HA2 subunits of influenza A HA with the aim to inhibit influenza A virus infection. The peptides were synthetized and their antiviral activity was tested in vitro against several influenza A viral strains: Puerto Rico/916/34 (H1N1), (H1N1)pdm09, swine (H1N1) and avian (H5N2). We found these peptides were able to inhibit the influenza A viral strains tested, without showing any cytotoxic effect. By docking studies we found evidence that all the peptides were capable to bind to the viral HA, principally to important regions on the viral HA stalk, thus could prevent the HA conformational changes required to carry out its membranes fusion activity.
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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.