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Cecropin A
Cat. No. AM-080
Structure:
H-Lys-Trp-Lys-Leu-Phe-Lys-Lys-Ile-Glu-Lys-Val-Gly-Gln-Asn-Ile-Arg-Asp-Gly-Ile-Ile-Lys-Ala-Gly-Pro-Ala-Val-Ala-Val-Val-Gly-Gln-Ala-Thr-Gln-Ile-Ala-Lys-NH2
Other Names:
CeA
Activity:
Broad spectrum insect antimicrobial
Cecropin A (CeA) is a natural linear cationic α-helical antimicrobial peptide (AMP) originally identified in moths (Hyalophora cecropia) and later in pig intestine. Cecropin A contains a strongly cationic region at its N-terminus and a large hydrophobic tail at its C-terminus, which allow its interaction with the microbial membrane, and then cell lysis by pore formation. Cecropin A has a wide spectrum of antimicrobial activities against gram-negative bacteria, gram-positive bacteria, and fungal phytopathogens. Cecropins constitute a main part of the innate immune system of insects.
Kulagina et al (2007) Antimicrobial peptides as new recognition molecules for screening challenging species. Sens. Actuators B Chem. 121(1) 150 PMID: 18231571
Yu et al (2016) Combination Effects of Antimicrobial Peptides. Antimicrob. Agents and Chemother. 60 (3) 1717 PMID: 26729502
Fratini et al (2025) Evaluation of the Synergistic Antimicrobial Activity of Essential Oils and Cecropin A Natural Peptide on Gram-Negative Bacteria. Animals 15 282 https://doi.org/10.3390/ani15020282
Related areas
All antimicrobial peptides >
All antifungal agents >
All immunology research categories >
Technical Data
| Structure | H-Lys-Trp-Lys-Leu-Phe-Lys-Lys-Ile-Glu-Lys-Val-Gly-Gln-Asn-Ile-Arg-Asp-Gly-Ile-Ile-Lys-Ala-Gly-Pro-Ala-Val-Ala-Val-Val-Gly-Gln-Ala-Thr-Gln-Ile-Ala-Lys-NH2 |
| CAS Number | 80451-04-3 |
| Molecular Weight | 4003.8 |
| Formula | C184H313N53O46 |
| Sequence | KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK-NH2 |
| Modifications | C terminal amide |
Solubility and Storage
| Solubility | Soluble in dilute acid |
| Appearance | Freeze dried solid |
| Storage | Store desiccated, frozen and in the dark |
Batch Specific Data
| Purity | >95% by HPLC |
| Safety Data Sheet | Cecropin A MSDS_602bac10175ca.pdf |
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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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