ArticleMarine drugs2018
A Novel Natural Influenza A H1N1 Virus Neuraminidase Inhibitory Peptide Derived from Cod Skin Hydrolysates and Its Antiviral Mechanism.
Article in Marine drugs, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 13 citations in OpenAlex.
- Targeting the Cardiovascular-Alzheimer's Disease Axis: The Promise of Marine Bioactive Peptides.Marine drugs · 2026Review
- Advances in Discovery and Design of Anti-influenza Virus Peptides.Current medicinal chemistry · 2026Review
- Bioactivity of Marine-Derived Peptides and Proteins: A Review.Marine drugs · 2025Review
- Antiviral strategies against influenza virus: an update on approved and innovative therapeutic approaches.Cellular and molecular life sciences : CMLS · 2025Review
- Development and characterization of an antibody that recognizes influenza virus N1 neuraminidases.PloS one · 2024Article
- Arbidol: The current demand, strategies, and antiviral mechanisms.Immunity, inflammation and disease · 2023Review
- Antiviral Peptides as Anti-Influenza Agents.International journal of molecular sciences · 2022Review
- Bioactive Antimicrobial Peptides: A New Weapon to Counteract Zoonosis.Microorganisms · 2022Review
- Advances in the stability challenges of bioactive peptides and improvement strategies.Current research in food science · 2022Review
- Peptides to combat viral infectious diseases.Peptides · 2020Review
- Comprehensive overview of COVID-19 based on current evidence.Dermatologic therapy · 2020Review
- Structure, Function, and Therapeutic Potential of Marine Bioactive Peptides.Marine drugs · 2019Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this paper, a novel natural influenza A H1N1 virus neuraminidase (NA) inhibitory peptide derived from cod skin hydrolysates was purified and its antiviral mechanism was explored. From the hydrolysates, novel efficient NA-inhibitory peptides were purified by a sequential approach utilizing an ultrafiltration membrane (5000 Da), sephadex G-15 gel column and reverse-phase high-performance liquid chromatography (RP-HPLC). The amino acid sequence of the pure peptide was determined by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICR-MS) was PGEKGPSGEAGTAGPPGTPGPQGL, with a molecular weight of 2163 Da. The analysis of the Lineweacer⁻Burk model indicated that the peptide was a competitive NA inhibitor with Ki of 0.29 mM and could directly bind free enzymes. In addition, docking studies suggested that hydrogen binding might be the driving force for the binding affinity of PGEKGPSGEAGTAGPPGTPGPQGL to NA. The cytopathic effect reduction assay showed that the peptide PGEKGPSGEAGTAGPPGTPGPQGL protected Madin⁻Darby canine kidney (MDCK) cells from viral infection and reduced the viral production in a dose-dependent manner. The EC
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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.