ArticleInternational journal of molecular sciences2021
The Potential Antimicrobial Action of Human Mucin 7 15-Mer Peptide and Its Metal Complexes.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Beyond proteolysis: rational modification of mucin-derived peptidomimetics with enhanced metal-mediated antimicrobial activity.RSC advances · 2026Article
- Dysregulated glycosaminoglycan biosynthesis and retinoid metabolism in chronic rhinosinusitis with nasal polyps: insights from a comprehensive transcriptomic analysis.Frontiers in immunology · 2026Article
- Recent Insights into the Potential and Challenges of Sericin as a Drug Delivery Platform for Multiple Biomedical Applications.Pharmaceutics · 2025Review
- A Case of Acquired Idiopathic Generalized Anhidrosis with Anti-mucin 7 Seropositivity.Acta dermato-venereologica · 2025Article
- Insights into the Chemistry, Structure, and Biological Activity of Human Salivary MUC7 Fragments and Their Cu(II) and Zn(II) Complexes.Inorganic chemistry · 2024Article
- Exploring the Correlation between Salivary Spinnbarkeit and Caries Scores.Caries research · 2024Article
- Rationally Designed Antimicrobial Peptides Are Potential Tools to Combat Devastating Bacteria and Fungi.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mucin 7 (encoded byMUC7) is a human salivary protein that has a role in the natural immune system. Fragments of mucin 7 exhibit antimicrobial activity against bacteria and yeast. Although the antimicrobial properties of peptides have been known and studied for decades, the exact mechanism of action of antimicrobial peptides (AMPs) is still unclear. It is known that some AMPs require divalent metal ions to activate their activity. Herein, we investigated three 15-mer MUC7 peptides, one of which (mother peptide, sequence, L3) is a synthetic analog of a fragment naturally excised from MUC7 (with His3, His8, and His 14) and its two structural analogs, containing only two histidine residues, His3, His13 and His8, His13 (L2 and L1, respectively). Since there is a correlation between lipophilicity, the presence of metal ions (such as Cu(II) and Zn(II)) and antimicrobial activity of AMP, antimicrobial properties of the studied peptides, as well as their complexes with Cu(II) and Zn(II) ions, were tested for activity against Gram-positive (
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Registered trials
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