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Cecropin A is a 37-residue cationic antimicrobial peptide originally characterized from the cecropia moth, Hyalophora cecropia. The mature peptide contains a C-terminal amide and a characteristic helix–hinge–helix architecture associated with membrane interaction.
Its sequence is strongly basic overall, supporting preferential association with negatively charged bacterial membrane surfaces.
Product Information
| Property | Specification |
|---|---|
| Product Name | Cecropin A |
| Catalog No. | AS2660 |
| CAS No. | 80451-04-3 |
| Sequence | 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 |
| One-Letter Sequence | KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK-NH₂ |
| Peptide Length | 37 amino acids |
| Molecular Formula | C184H313N53O46 |
| Molecular Weight | Approximately 4003.8 Da |
| C-Terminus | Amide |
| Peptide Class | Cationic insect antimicrobial peptide |
| Purity | Crude to 98% |
Helix–Hinge–Helix Architecture
Cecropin A contains two helical regions separated by a flexible Gly-Pro-containing hinge. The N-terminal segment is strongly amphipathic and cationic, while the C-terminal segment contributes a more hydrophobic surface.
This organization allows the peptide to associate with lipid bilayers without requiring a rigid globular structure. Membrane-bound studies have shown that both helical regions can orient approximately parallel to the membrane surface.
The hinge should therefore be considered an important structural element when designing shortened Cecropin A derivatives or hybrid antimicrobial peptides.
Membrane Permeabilization Research
Single-cell studies in E. coli have shown that Cecropin A can permeabilize the outer and cytoplasmic membranes in distinct stages rather than producing immediate homogeneous lysis across the entire cell surface.
Initial membrane disruption can be spatially localized, and peptide concentration influences whether measurable permeabilization occurs. These observations make Cecropin A useful for experiments examining threshold-dependent AMP action and membrane heterogeneity.
Research Applications
Cecropin A can support bacterial membrane studies, antimicrobial peptide SAR, lipid-vesicle experiments, hybrid peptide design and comparison of N-terminal versus C-terminal sequence contributions.
Researchers comparing closely related insect peptides can also review Cecropin B.
Synthetic and Quality Considerations
The 37-residue sequence and C-terminal amide should be confirmed when comparing synthetic Cecropin A with fragments, non-amidated constructs or cecropins derived from other species.
For sensitive biological studies, researchers can review our Recommended Peptide Purity guidance before selecting a specification.
Frequently Asked Questions
How many residues are in Cecropin A?
The mature Cecropin A sequence listed here contains 37 amino-acid residues.
Is Cecropin A C-terminally amidated?
Yes. The mature peptide contains a C-terminal Lys-NH₂.
Does Cecropin A simply form permanent membrane pores?
Its behavior is more complex. Membrane binding, localized permeabilization and threshold-dependent disruption have been observed, and the dominant mechanism can vary with the experimental system.