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| Description | Gramicidin C (CAS: 9062-61-7; 11-L-Tyr-gramicidin A) is a component of the gramicidin complex from Bacillus brevis: a 15-residue linear peptide with N-terminal formyl group and C-terminal ethanolamine ester, composed of alternating L- and D-amino acids. Molecular formula C98H141N19O18, MW 1873.30 Da. Gramicidin C differs from Gramicidin A by Tyr-for-Trp at position 11. In membranes, two gramicidin molecules align head-to-head to form a beta-helical transmembrane dimer that acts as a monovalent cation channel selective for H+, Na+, and K+, collapsing bacterial membrane potential. Gramicidin C is a classic biophysical model for membrane ion channels and has anti-Gram-positive activity. |
| Structure type | Linear 15-mer (alternating L/D, N-formyl + C-ethanolamide, ion-channel former) |
| Solubility | Readily soluble in ethanol, methanol |
| Storage | Powder -20C, dry, protected from light |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Gramicidin C | Gramicidin C1; 11-L-phenylalanine-gramicidin A; linear gramicidin (CAS 9062-61-7) | Ion channel peptide, Gramicidin, Bacillus brevis, alternating L/D amino acids, N-formylated, C-terminal ethanolamide, highly hydrophobic, transmembrane channel, anti-Gram-positive | 15-residue linear highly hydrophobic channel-forming peptide from Brevibacillus brevis; sequence formyl-L-Val-Gly-L-Ala-D-Leu-L-Ala-D-Val-L-Val-D-Val-L-Trp-D-Leu-L-Phe-D-Leu-L-Trp-D-Leu-L-Trp-ethanolamine; strictly alternating L/D stereochemistry, N-terminus formylated, C-terminus linked to ethanolamine; position 11 is Phe (distinguished from Trp11 in Gramicidin A and Tyr11 in Gramicidin B); two monomers dimerize N-to-N within the membrane to form a right-handed beta-helical transmembrane cation channel | C97H139N19O18 | 1858.05 | 1859.29 | TFA salt (trifluoroacetate); formula and MW calculated for free peptide | 15 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-GRAMC-01 | White to off-white crystalline powder | Store sealed, dry and protected from light at -20°C; light-sensitive due to multiple Trp residues; avoid repeated freeze-thaw | Ship/place short-term at 2-8°C; aliquotted working solution at -20°C | Extremely hydrophobic, practically insoluble in water: first dissolve fully in DMSO or absolute ethanol (~10 mg/mL), then dilute with buffer; Trp residues are photo-oxidation sensitive - protect solution from light; do not dissolve directly in water | solid is stable; tolerates short-term room-temperature shipping; long-term storage dry, dark at -20°C |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-GRAMC-01 | 15-residue alternating L/D amino acid channel-forming peptide from Brevibacillus brevis, N-formylated and C-terminal ethanolamide, Phe11 variant, dimerizes in membranes to form a transmembrane cation channel. | Gramicidin C is a linear pentadecapeptide antibiotic produced by Brevibacillus brevis, a component of the Gramicidin D mixture alongside Gramicidins A and B; it differs by having Phe at position 11 (Trp in A, Tyr in B). Its strictly alternating L/D stereochemistry, N-formyl block and C-terminal ethanolamide allow two monomers to dimerize N-to-N (head-to-head) within the lipid bilayer, forming a right-handed beta-helical transmembrane pore. This channel is selectively permeable to monovalent cations (Na+, K+), dissipating bacterial transmembrane ion gradients and membrane potential to kill cells, mainly against Gram-positive bacteria. Gramicidin C is a classic model tool in ion channel biophysics (single-channel conductance, membrane potential, lipid-peptide interactions), widely used in patch-clamp studies, artificial lipid bilayer recordings and drug delivery research. Owing to strong hemotoxicity, it is used only topically (e.g., eye ointments, skin infections) and not systemically. | Ion channel biophysics, Transmembrane transport, Patch-clamp/artifact bilayer, Antibiotic research, Membrane-lipid interactions, Peptide drug delivery | Cell membrane lipid bilayer; transmembrane monovalent cation channel (Na+/K+ permeation) |
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