ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2015
Cm-p5: an antifungal hydrophilic peptide derived from the coastal mollusk Cenchritis muricatus (Gastropoda: Littorinidae).
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 49 citations in OpenAlex.
- Natural and Synthetic AMPs from Latin America across Diversity Engineering and Applications.ACS infectious diseases · 2026Review
- Multiscale Modeling of the Bacterial Ribosome to Identify Potential Peptide Modulators and Their Allosteric Effects.Biochemistry · 2026Article
- Cm-p5, a synthetic antimicrobial peptide shows anti-Trypanosoma cruzi activity.PLoS neglected tropical diseases · 2026Article
- Unlocking Antimicrobial Peptides from Marine Invertebrates: A Comprehensive Review of Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2025Review
- Anti-biofilm peptides can rescue fluconazole and amphotericin B efficacies against Candida albicans.Scientific reports · 2025Article
- The Invertebrate-Derived Antimicrobial Peptide Cm-p5 Induces Cell Death and ROS Production in Melanoma Cells.Marine drugs · 2025Article
- Bioactivity of Marine-Derived Peptides and Proteins: A Review.Marine drugs · 2025Review
- Biofilm-Associated Candidiasis: Pathogenesis, Prevalence, Challenges and Therapeutic Options.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Structural Characterization of the Dimers and Selective Synthesis of the Cyclic Analogues of the Antimicrobial Peptide Cm-p5.Antibiotics (Basel, Switzerland) · 2025Article
- Aquatic Invertebrate Antimicrobial Peptides in the Fight Against Aquaculture Pathogens.Microorganisms · 2025Review
- Marine Antimicrobial Peptides: An Emerging Nightmare to the Life-Threatening Pathogens.Probiotics and antimicrobial proteins · 2024Review
- The Designed Pore-Forming Antimicrobial Peptide C14R Combines Excellent Activity against the Major Opportunistic Human PathogenPharmaceuticals (Basel, Switzerland) · 2024Article
- Cm-p5 Peptide Dimers Inhibit Biofilms ofInternational journal of molecular sciences · 2023Article
- Aptamers as Novel Binding Molecules on an Antimicrobial Peptide-Armored Composite Hydrogel Wound Dressing for Specific Removal and Efficient Eradication ofInternational journal of molecular sciences · 2023Article
- Identification and characterization of antimicrobial peptide (AMP) candidate from Gonggong Sea Snail (Journal of food science and technology · 2023Article
- Article
- Emerging and future strategies in the management of recalcitrant Candida auris.Medical mycology · 2022Review
- Discovery, Optimization, and Clinical Application of Natural Antimicrobial Peptides.Biomedicines · 2021Review
- Activity and Mechanism of Action of Antifungal Peptides from Microorganisms: A Review.Molecules (Basel, Switzerland) · 2021Review
- Antimicrobial Activity of Cyclic-Monomeric and Dimeric Derivatives of the Snail-Derived Peptide Cm-p5 against Viral and Multidrug-Resistant Bacterial Strains.Biomolecules · 2021Article
Corrections and comments
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Authors and funding
18 authors at 7 institutions in 5 countries.
Funding
Abstract
Antimicrobial peptides form part of the first line of defense against pathogens for many organisms. Current treatments for fungal infections are limited by drug toxicity and pathogen resistance. Cm-p5 (SRSELIVHQRLF), a peptide derived from the marine mollusk Cenchritis muricatus peptide Cm-p1, has a significantly increased fungistatic activity against pathogenic Candida albicans (minimal inhibitory concentration, 10 µg/ml; EC50, 1.146 µg/ml) while exhibiting low toxic effects against a cultured mammalian cell line. Cm-p5 as characterized by circular dichroism and nuclear magnetic resonance revealed an α-helical structure in membrane-mimetic conditions and a tendency to random coil folding in aqueous solutions. Additional studies modeling Cm-p5 binding to a phosphatidylserine bilayer in silico and isothermal titration calorimetry using lipid monophases demonstrated that Cm-p5 has a high affinity for the phospholipids of fungal membranes (phosphatidylserine and phosphatidylethanolamine), only moderate interactions with a mammalian membrane phospholipid, low interaction with ergosterol, and no interaction with chitin. Adhesion of Cm-p5 to living C. albicans cells was confirmed by fluorescence microscopy with FITC-labeled peptide. In a systemic candidiasis model in mice, intraperitoneal administration of Cm-p5 was unable to control the fungal kidney burden, although its low amphiphaticity could be modified to generate new derivatives with improved fungicidal activity and stability.
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