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| Description | Indolicidin (CAS: 140896-21-5) is a 13-residue cationic tryptophan-rich antimicrobial peptide purified from bovine neutrophil large cytoplasmic granules, C-terminally amidated, sequence Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2. Free-base formula C100H132N26O13, MW 1906.28 Da; TFA salt C102H133F3N26O15, MW 2020.31 Da. Indolicidin contains 5 tryptophans (38% of residues), making it one of the shortest cathelicidin family members, with a net +4 charge at physiological pH and potent activity against Gram-positive/Gram-negative bacteria, fungi, and protozoa. Its Trp-rich Pro-Trp motif confers strong membrane affinity, acting by membrane disruption and DNA binding. Indolicidin is a classic tool for the shortest active mammalian cathelicidin and Trp-rich membrane-active peptide SAR. |
| Structure type | Linear 13-mer (C-amidated bovine cathelicidin-4, Trp-rich, TFA salt) |
| Solubility | Readily soluble in water (>=1 mg/mL), 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) |
| Indolicidin TFA | Indolicidin; ILPWKWPWWPWRR-NH2; bovine neutrophil cathelicidin; CATH-4; triskelion AMP | cathelicidin AMP, tryptophan-rich peptide, C-terminal amidated, cationic peptide, anti-Gram-positive, anti-Gram-negative, antifungal, antiviral, bovine neutrophil-derived, light-sensitive | Linear 13-aa cationic peptide, sequence ILPWKWPWWPWRR (Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg), isolated from bovine (Bos taurus) neutrophil granule cathelicidin precursor; C-terminal Arg amidated; 1 Lys and 2 Arg plus free N-terminus, net charge ~+4; ~77% hydrophobic residues including 5 Trp, 3 Pro, Ile/Leu; 5 tryptophan residues (Trp-rich); no Cys, no disulfide, no Met, no His; does not form a canonical alpha-helix, adopts extended/turn conformation; Trp-rich face drives strong membrane insertion | C100H132N26O13 | 1905.05 | 1906.33 | TFA (trifluoroacetate); formula and MW calculated for free peptide (with C-terminal amide) | 13 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-INDOL-01 | White to pale yellow powder (may be pale yellow due to high Trp content) | -20°C, desiccated, sealed, strictly light-protected; 5 Trp residues are highly prone to photo-oxidation and oxidative degradation; wrap in aluminum foil, flush with argon/nitrogen; avoid repeated freeze-thaw | 2-8°C, desiccated, light-protected, stable for 1-2 weeks | Highly hydrophobic Trp-rich peptide (77% hydrophobic residues); low aqueous solubility; first prepare a stock in a small volume of DMSO or dilute acetic acid (0.1-1%), then dilute into aqueous buffer; due to extreme Trp photo-oxidation sensitivity, use amber tubes, prepare fresh, flush with argon, and use within 48 h | solid prone to oxidative discoloration and degradation due to 5 Trp residues; store strictly light-protected, dry, cold, and sealed; use promptly after opening |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-INDOL-01 | A 13-aa Trp-rich cathelicidin AMP from bovine neutrophils (ILPWKWPWWPWRR-NH2), C-terminally amidated, net charge +4; contains 5 Trp, strongly hydrophobic, kills via membrane disruption; highly light/oxidation-sensitive. | Indolicidin is a cathelicidin-family antimicrobial peptide isolated in the 1990s from bovine (Bos taurus) neutrophil azurophilic granules, processed from the CAMP precursor. At only 13 amino acids, it is one of the shortest known natural AMPs and is distinguished by an exceptionally high tryptophan content (5/13, ~38%). Its sequence ILPWKWPWWPWRR-NH2 clusters Trp residues in the middle and C-terminal half, while three Pro residues enforce a twisted, extended conformation rather than a canonical alpha-helix. With net charge +4 (1 Lys, 2 Arg, free N-terminus), the high Trp content drives potent hydrophobic membrane insertion. Indolicidin has broad activity against Gram-positive bacteria (including MRSA), Gram-negative bacteria, fungi (Candida albicans), and enveloped viruses (HIV-1, HSV). Beyond membrane permeabilization, it reportedly enters cells and inhibits DNA/RNA synthesis, suggesting additional intracellular targets. However, its high Trp content and strong hydrophobicity also confer substantial hemolytic and cytotoxic activity, limiting direct clinical use and motivating analog development (e.g., Varnerin, CP-10A4). Indolicidin is a classic model for studying Trp-rich membrane insertion, Pro-rich peptide conformation, and the hemolysis-versus-selectivity balance in short AMPs. | cathelicidin AMP biology, tryptophan-rich peptides, short peptide membrane disruption, anti-MRSA, antifungal, antiviral, hemolysis-selectivity balance, peptide drug lead discovery | bacterial membrane phospholipids, DNA/RNA synthesis (intracellular), fungal membranes, viral envelopes |
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