Antimicrobial · Linear α-helical cathelicidin
Mouse cathelicidin-related antimicrobial peptide (CRAMP)
Also known as mCRAMP; CRAMP; Camp-derived peptide
A 34-residue mouse cathelicidin used to examine membrane disruption, microbial-product binding and context-dependent Fpr2 signalling.
- Length
- 34 amino acids
- Half-life
- Not well characterised
- Mechanism
- CRAMP adopts an amphipathic α-helical structure in membrane-like environments and can permeabilise microbial membranes through electrostatic and hydrophobic interactions. Separately, formyl peptide receptor 2 (Fpr2)-dependent signalling has been reported in selected mouse cellular systems, while binding to microbial products can modify innate immune assay responses.
- Studied in
- Bacterial cultures, lipid vesicles, mouse leukocytes, epithelial cultures and Camp-deficient mouse models study CRAMP membrane activity and innate immune signalling.
About Mouse cathelicidin-related antimicrobial peptide (CRAMP)
Mouse CRAMP is the C-terminal antimicrobial peptide released from the cathelicidin precursor encoded by Camp. Its discovery through murine myeloid-cell studies established a mouse counterpart within the mammalian cathelicidin family. The precursor contains a conserved cathelin-like domain followed by the variable antimicrobial region. The commonly used mature research peptide has 34 residues and contains no cysteine, so its structure does not depend on disulphide bonds. It is distinct in sequence from human LL-37.
In aqueous solution CRAMP can be relatively disordered, whereas membrane-mimicking environments favour an amphipathic helix. This structural transition supports experiments on lipid selectivity, membrane leakage and bacterial envelope disruption. Beyond direct microbial interactions, studies examine binding to lipopolysaccharide and modulation of innate signalling. Fpr2 involvement has been reported in selected cellular responses, but should be tested within each model. Camp-deficient mice help distinguish endogenous cathelicidin contributions from the effects of isolated peptide in simplified assays.
Laboratory notes
- Confirm the 34-residue sequence and terminal chemistry; precursor fragments and modified analogues should be labelled separately.
- Measure endotoxin contamination and include peptide-only controls in leukocyte or reporter-cell experiments.
- Use receptor antagonism or genetic controls when assigning Fpr2 involvement, alongside viability and membrane-integrity readouts.
Storage and reconstitution basics: storage guide.
Questions about Mouse cathelicidin-related antimicrobial peptide (CRAMP)
Is CRAMP simply another name for LL-37?
No. CRAMP is the mouse cathelicidin-derived peptide, while LL-37 is a human cathelicidin-derived peptide. Their sequences, lengths and experimental behaviour differ.
Does CRAMP require disulphide formation?
No. The canonical 34-residue peptide contains no cysteine. Its membrane-associated conformation is mainly α-helical rather than disulphide-stabilised.
Is Fpr2 required for CRAMP antimicrobial activity?
Fpr2 signalling and direct antimicrobial activity are distinct mechanisms. Microbial membrane disruption does not require this mammalian receptor.
Is Mouse cathelicidin-related antimicrobial peptide (CRAMP) for human use?
No. It is supplied strictly for in-vitro laboratory research and is not for human or animal consumption.
Related research peptides
All products are sold for laboratory research use only. Not for human consumption, not a medicine, not for diagnosing, treating or preventing any condition.