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Cecropin B is a 35-amino-acid C-terminally amidated antimicrobial peptide originally characterized from the cecropia moth, Hyalophora cecropia.
Its sequence contains a strongly cationic N-terminal region, a more hydrophobic C-terminal segment and a central flexible region that together support interaction with bacterial lipid membranes.
Product Information
| Property | Specification |
|---|---|
| Product Name | Cecropin B |
| Catalog No. | AS2661 |
| CAS No. | 80451-05-4 |
| Sequence | Lys-Trp-Lys-Val-Phe-Lys-Lys-Ile-Glu-Lys-Met-Gly-Arg-Asn-Ile-Arg-Asn-Gly-Ile-Val-Lys-Ala-Gly-Pro-Ala-Ile-Ala-Val-Leu-Gly-Glu-Ala-Lys-Ala-Leu-NH₂ |
| One-Letter Sequence | KWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL-NH₂ |
| Peptide Length | 35 amino acids |
| Molecular Formula | C176H302N52O41S |
| Molecular Weight | Approximately 3834.7 Da |
| C-Terminus | Amide |
| Source Family | Insect cecropin peptide |
| Purity | Crude to 98% |
Domain Organization and Membrane Interaction
Cecropin B is not a uniformly hydrophobic peptide. Its N-terminal region is enriched in positively charged residues, while the C-terminal portion contains a larger hydrophobic contribution.
A flexible hinge between these regions allows the peptide to adapt its orientation at lipid interfaces. Molecular studies suggest that different Cecropin B molecules can cooperate during membrane interaction, with the amphipathic and hydrophobic segments contributing differently to insertion and membrane destabilization.
This domain organization makes Cecropin B useful for studying how a single linear peptide combines electrostatic recognition with hydrophobic membrane association.
C-Terminal Amidation
The mature Cecropin B sequence contains an amidated C-terminal Leu. Foundational biosynthetic work showed that the natural precursor includes a terminal glycine used in formation of the mature amide.
For synthetic material, we recommend treating the C-terminal amide as part of the defined molecular identity rather than as an optional generic modification.
Research Applications
Cecropin B can support studies of bacterial membrane permeabilization, antimicrobial peptide architecture, lipid selectivity and design of shortened or substituted AMP analogs.
For comparison with a longer member of the same family, researchers can review Cecropin A.
Quality and Experimental Planning
Sequence length, C-terminal amidation and molecular identity should be confirmed before quantitative comparisons with Cecropin B variants from other organisms or literature sources.
Our Peptide Quality Control capabilities support analytical HPLC and mass spectrometry with batch-specific documentation.
Frequently Asked Questions
How many amino acids are in Cecropin B?
The Cecropin B sequence listed here contains 35 amino-acid residues.
Is Cecropin B C-terminally amidated?
Yes. The mature sequence terminates in Leu-NH₂.
Can Cecropin B fragments or analogs be synthesized?
Truncations, residue substitutions and labeled constructs can be evaluated through Chemical Peptide Synthesis.