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| Description | Temporin A (CAS: 188713-69-1) is a 13-residue short cationic AMP isolated from skin granular secretion of the European common frog Rana temporaria, sequence FLPLIGRVLSGIL-NH2. Molecular formula C68H117N17O14, MW 1396.76 Da. A small, basic, highly hydrophobic amphipathic alpha-helix, Temporin A directly interacts with microbial membranes and shows broad activity against methicillin-sensitive and -resistant S. aureus (MRSA), vancomycin-resistant E. faecium (VRE), and Candida albicans, without erythrocyte toxicity at antimicrobial concentrations. Temporin A acts synergistically with temporin B in vivo for combined antibacterial and anti-inflammatory effects. It is a tool for amphibian short skin peptides, anti-drug-resistant Gram-positive membrane-active mechanisms, and peptide synergy. |
| Structure type | Linear 13-mer (C-amidated Rana temporaria skin cationic alpha-helical AMP) |
| Solubility | Readily soluble in DMSO, methanol, dilute acetic acid |
| 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) |
| Temporin A | Temporin A; FLPLIGRVLSGIL-NH2; Rana temporaria skin antimicrobial peptide; short alpha-helical frog AMP; CAS 188713-69-1 | antimicrobial peptide, frog skin peptide, Temporin family, short alpha-helical peptide, C-terminal amidated, strongly hydrophobic, cationic amphipathic peptide, anti-Gram-positive, Rana temporaria, 13-mer | Linear 13-aa peptide, sequence Phe1-Leu2-Pro3-Leu4-Ile5-Gly6-Arg7-Val8-Leu9-Ser10-Gly11-Ile12-Leu13-NH2 (FLPLIGRVLSGIL-NH2); Pro3 acts as an N-terminal hinge/breaker so that Phe1-Leu2-Pro3 adopts an extended/turn conformation, while residues Gly6-Leu4-Ile5 through Leu13 form an amphipathic alpha-helix; free N-terminus +1, Arg7 side-chain guanidinium +1, C-terminal amide carries no -1 charge, no acidic residues, net charge ~+2; hydrophobic residues (Phe, Leu x4, Ile x2, Val, Pro) ~69%, very hydrophobic; no Cys, Met, Trp, His, no disulfide; C-terminal amidation increases both net positive charge and membrane affinity/protease resistance | C68H117N17O14 | 1395.90 | 1396.79 | Free base; free N-terminal amine, C-terminal amidated (-CONH2), no counterion | 13 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-TEMPA-01 | White powder | -20°C, desiccated, sealed, light-protected; flush with argon/nitrogen; avoid repeated freeze-thaw | 2-8°C, desiccated and light-protected, stable for 1-2 weeks | Strongly hydrophobic cationic peptide (net +2, ~69% hydrophobic) with poor water solubility; pre-dissolve in DMSO or dilute acetic acid (0.1%) at 1-5 mg/mL stock, then dilute into aqueous buffers (PBS, Tris-HCl) to working concentration; DMSO stock can be aliquoted and stored at -20°C; prepare aqueous working solutions fresh to avoid aggregation/precipitation; no Cys/Met/Trp so no oxidation/photosensitivity, but concentrated aqueous solutions readily self-assemble | solid is stable and tolerates short-term ambient shipping; long-term storage dry at -20°C; highly hydrophobic peptides are hygroscopic and tend to cake; store under inert gas after opening |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-TEMPA-01 | A 13-aa short alpha-helical AMP from European common frog Rana temporaria skin (FLPLIGRVLSGIL-NH2), C-amidated, net +2, strongly hydrophobic; membrane-lytic against Gram-positive (incl. S. aureus) and some Gram-negative bacteria. | Temporin A is the prototypical member of the Temporin family, isolated from skin secretions of the European common frog Rana temporaria, with sequence Phe-Leu-Pro-Leu-Ile-Gly-Arg-Val-Leu-Ser-Gly-Ile-Leu-NH2 (13 aa). It is one of the shortest naturally occurring alpha-helical antimicrobial peptides. The Temporin family, systematically characterized by Simmaco and co-workers in the 1990s, comprises Temporins A, B, L and related peptides-all 10-14 aa, highly hydrophobic, C-terminally amidated cationic amphipathic peptides that constitute the first chemical line of amphibian skin innate defense. Temporin A has a distinctive architecture: Pro3 serves as an N-terminal hinge so that Phe1-Leu2-Pro3 do not helix, whereas residues Gly6-Leu4-Ile5 through Leu13 fold into a classic amphipathic alpha-helix at membrane interfaces-Arg7 lies on the cationic face, while Phe1/Leu2/Leu4/Ile5/Leu9/Val8/Ile12/Leu13 form the hydrophobic insertion face. Its mechanism is canonical membrane targeting: the cationic face electrostatically engages anionic bacterial headgroups (phosphatidylglycerol, cardiolipin, LPS), and the hydrophobic face inserts into the bilayer, causing depolarization, permeabilization and content leakage via carpet or barrel-stave models, ultimately killing the bacterium. Temporin A is active against Gram-positive bacteria (S. aureus, streptococci, enterococci) at single-digit microgram/mL MIC, and also shows some activity against Gram-negative bacteria and fungi; its short length and C-terminal amidation confer higher resistance to trypsin/chymotrypsin than non-amidated analogs, with relatively low hemolysis compared with longer amphipathic peptides (a favorable therapeutic window). Recent work demonstrates synergistic antibacterial and anti-inflammatory effects between Temporin A and Temporins B/L, suppressing growth at low combined concentrations and down-regulating LPS-induced TNF-alpha and IL-6, suggesting development potential against drug-resistant infections, local anti-infective dressings, wound healing, and peptide-antibiotic combination therapy. As a tool peptide, Temporin A is widely used as a model short alpha-helical membrane-acting AMP, for structure-activity studies of how a Pro hinge controls helix initiation and activity, for quantifying the contribution of C-terminal amidation to antibacterial potency and protease stability, and for comparative studies of amphibian innate immunity. | amphibian innate immunity, frog-skin AMPs, Temporin family, short alpha-helical membrane mechanisms, C-terminal amidation, anti-drug-resistant Gram-positive, peptide-antibiotic synergy, local anti-infective/wound dressing | Bacterial plasma membrane (PG/cardiolipin/LPS anionic headgroups); membrane depolarization and permeabilization; synergistic anti-inflammatory axis with Temporin B/L |
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