ArticleProbiotics and antimicrobial proteins2022
Serum Stable and Low Hemolytic Temporin-SHa Peptide Analogs Disrupt Cell Membrane of Methicillin-Resistant Staphylococcus aureus (MRSA).
Article in Probiotics and antimicrobial proteins, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Evaluation of Antileishmanial and Antibacterial Activity of Bioconjugate Guanidine-Temporin.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Antimicrobial peptides-based strategies at the frontline in battling the escalating menace of methicillin-resistant Staphylococcus aureus biofilms.European journal of microbiology & immunology · 2026Review
- Poly(ethylene Glycol)-Based Peptidomimetics (Pegtides) of Antimicrobial Peptides.Chembiochem : a European journal of chemical biology · 2025Article
- Pigments with antimicrobial and cytotoxic activities from the coprophilous fungusRSC advances · 2025Article
- Article
- Synthesis of Temporin-SHa Retro Analogs with Lysine Addition/Substitution and Antibiotic Conjugation to Enhance Antibacterial, Antifungal, and Anticancer Activities.Antibiotics (Basel, Switzerland) · 2024Article
- Synthesis of Second-Generation Analogs of Temporin-SHa Peptide Having Broad-Spectrum Antibacterial and Anticancer Effects.Antibiotics (Basel, Switzerland) · 2024Article
- Temporins: Multifunctional Peptides from Frog Skin.International journal of molecular sciences · 2023Review
- Design, Synthesis and Characterization of [G10a]-Temporin SHa Dendrimers as Dual Inhibitors of Cancer and Pathogenic Microbes.Biomolecules · 2022Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anti-microbial peptides (AMPs) have attracted major attention due to their potential bio-activities against some multidrug resistant pathogens. The present study evaluated the mechanism of actions of highly potent AMP temporin-SHa analogs, i.e., [G4a]-SHa, [G7a]-SHa, and [G10a]-SHa, against methicillin-resistant Staphylococcus aureus (MRSA) NCTC (13277) with minimum inhibitory concentrations (MICs) of 14.35, 7.16, and 3.58 µM, respectively. These analogs exhibited significant anti-MRSA activity at physiological salt concentration, 30% fetal bovine serum, and 30% human serum. [G4a]-SHa and [G7a]-SHa were non-hemolytic and non-cytotoxic to normal mouse fibroblast 3T3 cell and human Caco-2 cell line. Atomic force microscopy revealed that these analogs have profound effect on the morphological changes in MRSA surface with significant leakage of cell cytoplasmic content. Propidium iodide uptake kinetic assay and (bis-(1,3-dibutylbarbituric acid) trimethine oxonol) DiBAC
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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.