Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (681 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
A group of peptide antibiotics from bacillus brevis. Gramicidin C or S is a cyclic, ten-amino acid polypeptide and gramicidins A, B, D are linear. Gramicidin is one of the two principal components of tyrothricin.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Gramicidins; Gramicidin A(1); Linear Gramicidin; Gramicidin, Linear; Gramicidin D; Gramicidin Dubos; Gramicidin K; Gramicidin P.
Where it fits in the MeSH classification
- Broader topics
- Tyrothricin; Pore Forming Cytotoxic Proteins
Related concepts
- Bacillus
- Tyrothricin
Research landscape
PubMed indexes 2,793 records tagged with the MeSH heading “Gramicidin” (counts retrieved 2026-10-31). 108 of them (3.9%) were published from 2020 onward, and the busiest period so far is through 1999 with 1,759 records.
Reviews account for 138 records (4.9%) and meta-analyses for 1. Randomized controlled trials number 26 (0.9%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 1,759 |
| 2000-2009 | 593 |
| 2010-2019 | 333 |
| 2020 onward | 108 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 138 | 4.9% |
| Meta-analyses | 1 | 0.0% |
| Randomized controlled trials | 26 | 0.9% |
Method: PubMed query "Gramicidin"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in drugs and chemicals
Studies of a chemical or drug can answer very different questions: what it is and how it behaves in cells and animals, how the body handles it, and whether it changes outcomes in people. Laboratory and animal findings often do not carry over to patients, and observational studies of exposures are confounded by who uses a substance and why. Nothing on this page is a recommendation to use, avoid, start or stop any substance or medicine; talk to a qualified clinician or pharmacist about your own situation. Check the dose, the species, the comparison group and whether a patient-relevant outcome was measured.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Structure, toxicity and antibiotic activity of gramicidin S and derivatives | 2016 | Research article Design not recorded in structured metadata | 48 | cc by PMID 26886453 · DOI · PMC4840228 |
| The antimicrobial activity of gramicidin A is associated with hydroxyl radical formation | 2015 | Research article Design not recorded in structured metadata | 46 | cc by PMID 25622083 · DOI · PMC4306519 |
| Discovery of gramicidin A analogues with altered activities by multidimensional screening of a one-bead-one-compound library | 2020 | Research article Design not recorded in structured metadata | 32 | cc by PMID 33004797 · DOI · PMC7531004 |
| Electric field-induced rupture kinetics of giant unilamellar vesicles with varying gramicidin A content in membrane | 2026 | Research article Design not recorded in structured metadata | 0 | cc by PMID 41490057 · DOI · PMC12768252 |
Structure, toxicity and antibiotic activity of gramicidin S and derivatives [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Development of new antibiotics is declining whereas antibiotic resistance is rising, heralding a post-antibiotic era.
- Closing excerpt
- Modification of GS enables production of novel derivatives potentially useful for systemic treatment of human infections.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (132 words)
Development of new antibiotics is declining whereas antibiotic resistance is rising, heralding a post-antibiotic era. Antimicrobial peptides such as gramicidin S (GS), exclusively topically used due to its hemolytic side-effect, could still be interesting as therapeutic compounds. By modifying the amino-acid composition of GS, we synthesized GS analogues. We now show that derivative VK7 has a lower MIC (7.8-31.2 μg/ml, median 15.6 μg/ml) against strains of multi-drug resistant (MDR) Klebsiella pneumoniae, Acinetobacter baumannii, and Pseudomonas aeruginosa than GS has (3.9-62.5 μg/ml, median 31.3 μg/ml). Low MICs for both VK7 and GS were observed for Staphylococcus aureus and Enterococcus faecium. VK7 showed reduced haemolysis and less lactate dehydrogenase release. All compounds were fully bactericidal at MIC values. Modification of GS enables production of novel derivatives potentially useful for systemic treatment of human infections.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 26886453 · DOI · PMC4840228
The antimicrobial activity of gramicidin A is associated with hydroxyl radical formation [2]
Abstract reading summary — source excerpts
- Opening excerpt
- Gramicidin A is an antimicrobial peptide that destroys gram-positive bacteria.
- Closing excerpt
- This new finding may provide insight into the underlying bactericidal mechanism of gA.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (191 words)
Gramicidin A is an antimicrobial peptide that destroys gram-positive bacteria. The bactericidal mechanism of antimicrobial peptides has been linked to membrane permeation and metabolism disruption as well as interruption of DNA and protein functions. However, the exact bacterial killing mechanism of gramicidin A is not clearly understood. In the present study, we examined the antimicrobial activity of gramicidin A on Staphylococcus aureus using biochemical and biophysical methods, including hydroxyl radical and NAD+/NADH cycling assays, atomic force microscopy, and Fourier transform infrared spectroscopy. Gramicidin A induced membrane permeabilization and changed the composition of the membrane. The morphology of Staphylococcus aureus during gramicidin A destruction was divided into four stages: pore formation, water permeability, bacterial flattening, and lysis. Changes in membrane composition included the destruction of membrane lipids, proteins, and carbohydrates. Most interestingly, we demonstrated that gramicidin A not only caused membrane permeabilization but also induced the formation of hydroxyl radicals, which are a possible end product of the transient depletion of NADH from the tricarboxylic acid cycle. The latter may be the main cause of complete Staphylococcus aureus killing. This new finding may provide insight into the underlying bactericidal mechanism of gA.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 25622083 · DOI · PMC4306519
Discovery of gramicidin A analogues with altered activities by multidimensional screening of a one-bead-one-compound library [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Gramicidin A (1) is a peptide antibiotic that disrupts the transmembrane ion concentration gradient by forming an ion channel in a lipid bilayer.
- Closing excerpt
- Our large-scale structure-activity relationship studies reveal the feasibility of developing analogues of 1 that selectively induce toxicity toward target organisms.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (147 words)
Gramicidin A (1) is a peptide antibiotic that disrupts the transmembrane ion concentration gradient by forming an ion channel in a lipid bilayer. Although long used clinically, it is limited to topical application because of its strong hemolytic activity and mammalian cytotoxicity, likely arising from the common ion transport mechanism. Here we report an integrated high-throughput strategy for discovering analogues of 1 with altered biological activity profiles. The 4096 analogue structures are designed to maintain the charge-neutral, hydrophobic, and channel forming properties of 1. Synthesis of the analogues, tandem mass spectrometry sequencing, and 3 microscale screenings enable us to identify 10 representative analogues. Re-synthesis and detailed functional evaluations find that all 10 analogues share a similar ion channel function, but have different cytotoxic, hemolytic, and antibacterial activities. Our large-scale structure-activity relationship studies reveal the feasibility of developing analogues of 1 that selectively induce toxicity toward target organisms.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 33004797 · DOI · PMC7531004
Electric field-induced rupture kinetics of giant unilamellar vesicles with varying gramicidin A content in membrane [4]
Abstract reading summary — source excerpts
- Opening excerpt
- In this study, we examine the rupture kinetics of giant unilamellar vesicles (GUVs) composed of DOPG/DOPC and varying mole fractions of gramicidin A (GrA), under externally applied electric fields.
- Closing excerpt
- This study provides new insights into the tunable electromechanical properties of lipid membranes modulated by membrane-active peptides.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (211 words)
In this study, we examine the rupture kinetics of giant unilamellar vesicles (GUVs) composed of DOPG/DOPC and varying mole fractions of gramicidin A (GrA), under externally applied electric fields. Time-resolved fluorescence microscopy reveals that the presence of GrA modulates vesicle rupture behavior in a non-monotonic fashion. At lower contents of GrA (0-0.05 mole%), GUVs exhibit enhanced structural resilience, with significantly reduced rupture probability, suggesting increased membrane stability. However, at higher contents of GrA (0.05-5%), vesicles display accelerated rupture kinetics, reflecting decreased membrane integrity. Quantitative analysis of rupture events indicates a biphasic dependence of the rupture rate constant on GrA content. The pore-edge tension was obtained from the slope of the fitted linear relation between the logarithm of the rupture rate constant and the inverse of effective membrane tension for different GrA%. The pore-edge tension varies nonlinearly with GrA%, reaching a minimum at intermediate GrA levels (0.05%). These findings are consistent with a theoretical model for electroporation, where pore formation is governed by a balance between destabilizing electric tension and stabilizing line tension. The results highlight how lower mole% of GrA enhance membrane mechanical robustness, while excessive GrA incorporation disrupts bilayer cohesion and accelerates electroporation. This study provides new insights into the tunable electromechanical properties of lipid membranes modulated by membrane-active peptides.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 41490057 · DOI · PMC12768252
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Bilayer thickness and membrane protein function: an energetic perspective [5]
- Research article Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes [6]
- Research article The gramicidin ion channel: a model membrane protein [7]
- Research article Model ion channels: gramicidin and alamethicin [8]
- Research article Gramicidin channels [9]
- Research article The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes [10]
References
- Swierstra J, Kapoerchan V, Knijnenburg A, van Belkum A, Overhand M. Structure, toxicity and antibiotic activity of gramicidin S and derivatives. . 2016. PMID 26886453 · DOI · PMC4840228
- Liou JW, Hung YJ, Yang CH, Chen YC. The antimicrobial activity of gramicidin A is associated with hydroxyl radical formation. . 2015. PMID 25622083 · DOI · PMC4306519
- Takada Y, Itoh H, Paudel A, Panthee S, Hamamoto H, Sekimizu K, et al.. Discovery of gramicidin A analogues with altered activities by multidimensional screening of a one-bead-one-compound library. . 2020. PMID 33004797 · DOI · PMC7531004
- Bhuiyan MTI, Ahamed MJ, Sultana R, Nasrin T, Ahamed MK, Billah MM, et al.. Electric field-induced rupture kinetics of giant unilamellar vesicles with varying gramicidin A content in membrane. . 2026. PMID 41490057 · DOI · PMC12768252
- Andersen OS, Koeppe RE. Bilayer thickness and membrane protein function: an energetic perspective. Annu Rev Biophys Biomol Struct. 2007. PMID 17263662 · DOI
- Lundbaek JA, Collingwood SA, Ingólfsson HI, Kapoor R, Andersen OS. Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes. J R Soc Interface. 2010. PMID 19940001 · DOI · PMC2842803
- Kelkar DA, Chattopadhyay A. The gramicidin ion channel: a model membrane protein. Biochim Biophys Acta. 2007. PMID 17572379 · DOI
- Woolley GA, Wallace BA. Model ion channels: gramicidin and alamethicin. J Membr Biol. 1992. PMID 1279177 · DOI
- Andersen OS. Gramicidin channels. Annu Rev Physiol. 1984. PMID 6201133 · DOI
- Prenner EJ, Lewis RN, McElhaney RN. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes. Biochim Biophys Acta. 1999. PMID 10590309 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-31.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.