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RW3
Cat. No. AM-150
Structure:
H-Arg-Trp-Arg-Trp-Arg-Trp-NH2
Activity:
Antimicrobial and antifungal
RW3 is a short peptide containing repeating arginine (R) and tryptophan (W) residues which has been shown to possess antimicrobial and antifungal activity with low cytotoxicity. The positively charged arginine interacts with the bacterial membrane through electrostatic attraction whereas the non-polar tryptophan residue interacts with the lipid bilayer. These two properties allow RW3 to interact with the bacterial membrane, resulting in membrane destabilization and pore formation and bacterial cell death. RW3 has been shown to have enhanced activity in combination with other antimicrobial agents.
Strøm et al (2002) Antimicrobial activity of short arginine- and tryptophan-rich peptides. J. Pept. Sci. 8(8) 431 PMID: 12212806
Liu et al (2007) Length effects in antimicrobial peptides of the (RW)n series. Antimicrob. Agents Chemother. 51(2) 597 PMID: 17145799
Mohan et al (2014) Enhanced antimicrobial activity of peptide-cocktails against common bacterial contaminants of ex vivo stored platelets. Clin. Microbiol. Infect. 20(1) O39 PMID: 23926880
Related areas
All antimicrobial peptides >
All antifungal agents >
All immunology research areas >
Technical Data
| Structure | H-Arg-Trp-Arg-Trp-Arg-Trp-NH2 |
| Molecular Weight | 1044.2 |
| Formula | C51H69N19O6 |
| Sequence | RWRWRW-NH2 |
| Modifications | C terminal amide |
Solubility and Storage
| Solubility | Soluble in dilute acid and physiological buffers |
| Appearance | Freeze dried solid |
| Storage | Store desiccated, frozen and in the dark |
Batch Specific Data
| Purity | >95% by HPLC |
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Recent citations
A new publication from the University of Ljubljana uses MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2, the FRET substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro), to determine the inhibitory potential of plant polyphenols
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