LL-37 – Human cathelicidin peptide – Potent antimicrobial peptide
LL-37, also known as CAP-18 for Cathelicidin antimicrobial peptide 18, is a 37 amino acid cationic peptide. LL-37 is also a typical linear antimicrobial peptide which can eliminate a wide range of pathogenes, including bacteria, viruses, fungi, and parasites. CAP-18 is the only human cathelicidin peptide reported yet, found in lysosomes of macrophages and leukocytes.
LL-37 plays an important role in the first act of defense against local infection and systemic invasion of pathogens at sites of inflammation.
CAP-18 shows cytotoxicity against bacterial and normal eukaryotic cells and is significantly resistant to proteolytic degradation. Besides its antimicrobial functions, CAP-18 also has immunomodulatory roles. LL-37 suppresses the production of pro-inflammatory cytokines, TNF-α and IL-6 in infected monocytes. CAP-18 increases cytokine and chemokine liberation from local cells and leucocytes and has chemotactic effects on a large number of immune cells.
SB-PEPTIDE offers the scrambled version of LL-37 peptide (see section “Scrambled LL-37 peptide”).
|Sequence : LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES|
|MW : 4 493.4 Da (C205H340N60O53)|
|Purity : > 95%|
|Counter-Ion : TFA Salts (see option TFA removal)|
|Delivery format : Freeze dried in propylene 2mL microtubes|
|Other names : Cathelicidin,154947-66-7, All38 peptide, BAC4, CAP18, CAMP,|
|Peptide Solubility Guideline|
|Bulk peptide quantities available|
|Product catalog||Size||Price € HT||Price $ USD|
1- Sheehan, Gerard et al. Infection and immunity vol. 86,7 e00097-18. (2018)
The Human Cathelicidin Antimicrobial Peptide LL-37 Promotes the Growth of the Pulmonary Pathogen Aspergillus fumigatus
BACKGROUND: The pulmonary mucus of cystic fibrosis (CF) patients displays elevated levels of the cathelicidin antimicrobial peptide LL-37.
OBJECTIVE: Assess the effect of LL-37 on the growth of Aspergillus fumigatus, a common pathogen of CF patients.
METHOD/RESULTS: Exposure of A. fumigatus to LL-37 and its derived fragment RK-31 (1.95 μg/ml) for 24 h had a positive effect on growth (199.94% ± 6.172% [P < 0.05] and 218.20% ± 4.63% [P < 0.05], respectively), whereas scrambled LL-37 peptide did not (85.12% ± 2.92%). Exposure of mycelium (preformed for 24 h) to 5 μg/ml intact LL-37 for 48 h increased hyphal wet weight (4.37 ± 0.23 g, P < 0.001) compared to the control (2.67 ± 0.05 g) and scrambled LL-37 (2.23 ± 0.09 g) treatments. Gliotoxin secretion from LL-37 exposed hyphae (169.1 ± 6.36 ng/mg hyphae, P < 0.05) was increased at 24 h compared to the results seen with the control treatment (102 ± 18.81 ng/mg hyphae) and the scrambled LL-37 treatment (96.09 ± 15.15 ng/mg hyphae). Shotgun proteomic analysis of 24-h LL-37-treated hyphae revealed an increase in the abundance of proteins associated with growth (eukaryotic translation initiation factor 5A [eIF-5A] [16.3-fold increased]), tissue degradation (aspartic endopeptidase [4.7-fold increased]), and allergic reactions (Asp F13 [10-fold increased]). By 48 h, there was an increase in protein levels indicative of cellular stress (glutathione peroxidase [9-fold increased]), growth (eIF-5A [6-fold increased]), and virulence (RNase mitogillin [3.7-fold increased]).
CONCLUSION: These results indicate that LL-37 stimulates A. fumigatus growth and that this stimulation can result in increased fungal growth and secretion of toxins in the lungs of CF patients.T