ll-37, human

LL-37, Human is a 37-residue, amphipathic, cathelicidin-derived antimicrobial peptide, which exhibits a broad spectrum of antimicrobial activity.

LL-37, Human acetate is a 37-residue, amphipathic, cathelicidin-derived antimicrobial peptide, which exhibits a broad spectrum of antimicrobial activity.

Human LL-37 is a 37 amino acid cationic (6+) peptide and has been widely studied. LL-37 penetrates the bacterial membrane and forms pores in the membrane.

LL-37 (18-37), an antimicrobial peptide fragment of LL-37, exhibits activity against S. aureus and C. albicans, with minimum lethal concentrations of 4 µM and 10 µM, respectively. Additionally, it inhibits E. histolytica trophozoites growth at concentrations between 10 to 50 µM.

β-Defensin-2 is a peptide with antimicrobial properties that protects the skin and mucosal membranes of the respiratory, genitourinary, and gastrointestinal tracts.1It inhibits the growth of periodontopathogenic and cariogenic bacteria, includingP. gingivalisandS. salivarius.2β-Defensin-2 (30 μg/ml) stimulates gene expression and production of IL-6, IL-10, CXCL10, CCL2, MIP-3α, and RANTES by keratinocytes.3It also stimulates calcium mobilization, migration, and proliferation of keratinocytes when used at concentrations of 30, 10, and 40 μg/ml, respectively. β-Defensin-2 induces IL-31 production by human peripheral blood-derived mast cellsin vitrowhen used at a concentration of 10 μg/ml and by rat mast cellsin vivofollowing a 500 ng intradermal dose.4Expression of β-defensin-2 is increased in psoriatic skin and chronic wounds.5,6 1.Lehrer, R.I.Primate defensinsNat. Rev. Microbiol.2(9)727-738(2004) 2.Ouhara, K., Komatsuzawa, H., Yamada, S., et al.Susceptibilities of periodontopathogenic and cariogenic bacteria to antibacterial peptides, β-defensins and LL37, produced by human epithelial cellsJ. Antimicrob. Chemother.55(6)888-896(2005) 3.Niyonsaba, F., Ushio, H., Nakano, N., et al.Antimicrobial peptides human β-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokinesJ. Invest. Dermatol.127(3)594-604(2007) 4.Niyonsaba, F., Ushio, H., Hara, M., et al.Antimicrobial peptides human β-defensins and cathelicidin LL-37 induce the secretion of a pruritogenic cytokine IL-31 by human mast cellsJ. Immunol.184(7)3526-3534(2010) 5.Huh, W.-K., Oono, T., Shirafuji, Y., et al.Dynamic alteration of human β-defensin 2 localization from cytoplasm to intercellular space in psoriatic skinJ. Mol. Med. (Berl.)80(10)678-684(2002) 6.Butmarc, J., Yufit, T., Carson, P., et al.Human β-defensin-2 expression is increased in chronic woundsWound Repair Regen.12(4)439-443(2004)

LL-37 GKE acetate, a peptide with 21 amino acids and the active structural domain of LL-37, inhibits lps-induced vascular nitric oxide production, is less toxic than LL-37 for hemolysis and apoptosis in human cultured smooth muscle cells, and possesses antimicrobial activity and therapeutic potential for sepsis.

Lugdunin is an antibiotic peptide that disrupts membrane potential in bacteria, demonstrating activity against Gram-positive species including S. aureus, and effectively reducing skin and nasal colonization of this pathogen. Moreover, Lugdunin stimulates the production of LL-37 and CXCL8 MIP-2 in human keratinocytes and mouse skin [1].

LL-37(17-32) is a biologically active peptide fragment derived from the C-terminal domain of human cathelicidin antimicrobial peptide. This segment reverses ABCG2-mediated multidrug resistance in cancer cell lines, highlighting its potential therapeutic role against drug resistance.

CRAMP (140-173) (mouse), the ortholog of the human LL-37 antimicrobial peptide, inhibits LPS-induced responses and does not colocalize with TLR3 in BEAS-2B cells [1].

Citrullinated LL-37 1cit, a modified LL-37 peptide, retains the antiviral properties of its parent compound against human rhinovirus and exhibits antibacterial activity against S. aureus. Furthermore, it diminishes the RV1B-induced expression of pro-inflammatory cytokines, including IL-8, CCL5, and IL-6 mRNA [1].

Citrullinated LL-37 2cit, a modified version of the LL-37 peptide, attenuates the antiviral efficacy of LL-37 against Human Rhinovirus (HRV) at a concentration of 10 μg mL and diminishes its antibacterial properties. Furthermore, the compound diminishes RV1B-induced mRNA expression of pro-inflammatory cytokines IL-8, CCL5, and IL-6, and demonstrates a moderate decline in suppressing HRV-stimulated CCL5 secretion [1].

Citrullinated LL-37 3cit is a host defense peptide with notable immunomodulatory and antimicrobial properties, which exhibits direct antiviral activity against human rhinoviruses (HRV) [1].