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| Description | Im6 is a short-chain cationic antimicrobial peptide with antimicrobial activity, sequence Phe-Phe-Phe-Leu-Pro-Ser-Leu-Ile-Gly-Gly-Leu-Val-Ser-Ala-Ile-Lys-NH2 (one-letter: FFFLPSLIGGLVSAIK-NH2), with the C-terminal carboxyl group amidated, totaling 16 amino acid residues, with a theoretical molecular weight of 1708.09 Da and molecular formula C86H134N18O18. The sequence of Im6 exhibits typical hydrophobic antimicrobial peptide characteristics: the N-terminus contains 3 consecutive phenylalanine residues (Phe-Phe-Phe, providing extremely strong hydrophobicity and membrane affinity for the peptide), and the overall sequence is rich in hydrophobic amino acids (3 phenylalanines, 3 leucines, 2 isoleucines, 1 proline, 1 alanine, 1 valine, 2 glycines), with only 1 positively charged lysine residue (Lys, at position 16) at the C-terminus, and a net charge of +1. This "strongly hydrophobic N-terminus + single positive charge C-terminus" structural characteristic enables Im6 to primarily bind to cell membranes through hydrophobic interactions. In a membrane environment, Im6 can form an amphipathic alpha-helical structure, inserting into the cell membrane lipid bilayer through the hydrophobic face. C-terminal amidation eliminates the negative charge of the C-terminal carboxyl group, increasing the peptide's membrane-binding ability. Im6 exhibits antimicrobial activity against Gram-positive bacteria, with bactericidal activity against Staphylococcus aureus and Bacillus subtilis. The antimicrobial mechanism of Im6 primarily involves disruption of bacterial cell membranes: as a cationic amphipathic peptide, Im6 inserts into the bacterial cell membrane lipid bilayer through the strong hydrophobicity of its N-terminal phenylalanine triplet, while the positive charge of the C-terminal lysine provides electrostatic interaction with negatively charged teichoic acids on the bacterial cell membrane surface (Gram-positive bacteria), leading to increased cell membrane permeability, depolarization, and content leakage, ultimately resulting in bacterial death. As a short-chain antimicrobial peptide, Im6 has the advantages of low synthesis cost, good tissue penetration, and easy modification, and is widely used in antimicrobial peptide structure-activity relationship research, alpha-helical antimicrobial peptide membrane action mechanism research, anti-Gram-positive bacteria drug development, hydrophobic antimicrobial peptide design research, and novel antibiotic lead compound screening. |
| Molecular weight (Da) | 1708.09 |
| Structure type | Linear 16-mer peptide (C-terminally amidated, cationic amphipathic short-chain antimicrobial peptide, N-terminal phenylalanine triplet with strong hydrophobicity, anti-Staphylococcus aureus and Bacillus subtilis) |
| Solubility | Readily soluble in water, PBS, DMSO |
| Storage | Powder at -20C, dry and 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) |
| Im6 | Indolicidin analog Im6; tryptophan-rich antifungal peptide | Antimicrobial peptide, antifungal peptide, tryptophan-rich peptide, skin anti-infection, biofilm inhibition | Short-chain antimicrobial peptide optimized and derived from indolicidin, rich in tryptophan and arginine; exerts dual activity by disrupting fungal cell membranes and inhibiting nucleic acid synthesis; effective against pathogenic fungi such as Candida and Gram-positive bacteria, and can inhibit biofilms | C₈₇H₁₀₃N₁₇O₉ | 1553.8 | ~1554.9 | Acetate | 13 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-IM6 | White powder | Store at -20°C, sealed, dry and protected from light. Aliquot for storage. | Stable for 1 month at 2–8°C in sealed dry condition; stable for shipping at ambient temperature. | Stable for 7 days at 4°C. Soluble in dilute acetic acid and acidic buffers. Tryptophan residues are prone to photooxidation and inactivation. Soluble and stable under acidic conditions; higher antifungal activity than linear indolicidin. | Stable for 2 years at -20°C, dry and protected from light. |
Functional Description
| Product Code | Frontend Short Summary (for search list display) | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-IM6 | Optimized Im6 indolicidin analog with dual antibacterial and antifungal activity | Im6 is an optimized derivative of the natural AMP indolicidin with improved stability and antifungal activity via sequence engineering. Rich in tryptophan and arginine, it disrupts fungal membrane integrity and inhibits intracellular nucleic acid synthesis, active against Candida and Gram-positive bacteria, and inhibits fungal biofilm formation. | Skin fungal infections, antifungal drug development, biofilm inhibition, indolicidin derivatives, natural peptide optimization | Fungal membrane integrity; fungal nucleic acid synthesis inhibition; tryptophan membrane insertion |
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