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LL-37 (scrambled)

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

LL-37 (scrambled) is the control peptide for LL-37.

Category

Functional Peptides

Catalog number

BAT-014768

CAS number

1354065-56-7

Molecular Formula

C205H340N60O53

Molecular Weight

4493.33

Specification
Reference Reading

IUPAC Name

(4S)-4-[[2-[[(2S)-6-amino-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[(2-aminoacetyl)amino]-4-methylpentanoyl]amino]hexanoyl]amino]-4-methylpentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-phenylpropanoyl]amino]-4-carboxybutanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]hexanoyl]amino]acetyl]amino]-5-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S,3R)-1-[(2S)-2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-1-[[(2S,3S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(1S)-4-carbamimidamido-1-carboxybutyl]amino]-1,5-dioxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-5-oxopentanoic acid

Synonyms

Cationic Antimicrobial Protein 18 (134-170) (Scrambled) (human); H-Gly-Leu-Lys-Leu-Arg-Phe-Glu-Phe-Ser-Lys-Ile-Lys-Gly-Glu-Phe-Leu-Lys-Thr-Pro-Glu-Val-Arg-Phe-Arg-Asp-Ile-Lys-Leu-Lys-Asp-Asn-Arg-Ile-Ser-Val-Gln-Arg-OH; hCAP-18 (134-170); glycyl-L-leucyl-L-lysyl-L-leucyl-L-arginyl-L-phenylalanyl-L-alpha-glutamyl-L-phenylalanyl-L-seryl-L-lysyl-L-isoleucyl-L-lysyl-glycyl-L-alpha-glutamyl-L-phenylalanyl-L-leucyl-L-lysyl-L-threonyl-L-prolyl-L-alpha-glutamyl-L-valyl-L-arginyl-L-phenylalanyl-L-arginyl-L-alpha-aspartyl-L-isoleucyl-L-lysyl-L-leucyl-L-lysyl-L-alpha-aspartyl-L-asparagyl-L-arginyl-L-isoleucyl-L-seryl-L-valyl-L-glutaminyl-L-arginine

Appearance

White Powder

Purity

≥95%

Sequence

GLKLRFEFSKIKGEFLKTPEVRFRDIKLKDNRISVQR

Storage

Store at -20°C

Solubility

Soluble in Water

InChI

InChI=1S/C205H340N60O53/c1-20-114(16)162(261-176(293)126(65-39-45-85-210)239-191(308)148(106-266)257-187(304)144(100-121-59-33-26-34-60-121)253-175(292)134(75-79-156(275)276)240-185(302)142(98-119-55-29-24-30-56-119)250-170(287)128(67-47-87-225-201(215)216)236-182(299)139(95-110(8)9)247-167(284)123(62-36-42-82-207)233-180(297)137(93-108(4)5)232-153(271)104-212)196(313)242-122(61-35-41-81-206)166(283)230-105-154(272)231-132(74-78-155(273)274)173(290)252-143(99-120-57-31-25-32-58-120)186(303)249-140(96-111(10)11)183(300)235-127(66-40-46-86-211)178(295)264-165(117(19)268)199(316)265-92-52-72-150(265)193(310)241-135(76-80-157(277)278)179(296)259-160(112(12)13)194(311)243-130(69-49-89-227-203(219)220)172(289)251-141(97-118-53-27-23-28-54-118)184(301)237-129(68-48-88-226-202(217)218)171(288)256-147(103-159(281)282)190(307)263-163(115(17)21-2)197(314)244-125(64-38-44-84-209)169(286)248-138(94-109(6)7)181(298)234-124(63-37-43-83-208)168(285)255-146(102-158(279)280)189(306)254-145(101-152(214)270)188(305)238-131(70-50-90-228-204(221)222)177(294)262-164(116(18)22-3)198(315)258-149(107-267)192(309)260-161(113(14)15)195(312)245-133(73-77-151(213)269)174(291)246-136(200(317)318)71-51-91-229-205(223)224/h23-34,53-60,108-117,122-150,160-165,266-268H,20-22,35-52,61-107,206-212H2,1-19H3,(H2,213,269)(H2,214,270)(H,230,283)(H,231,272)(H,232,271)(H,233,297)(H,234,298)(H,235,300)(H,236,299)(H,237,301)(H,238,305)(H,239,308)(H,240,302)(H,241,310)(H,242,313)(H,243,311)(H,244,314)(H,245,312)(H,246,291)(H,247,284)(H,248,286)(H,249,303)(H,250,287)(H,251,289)(H,252,290)(H,253,292)(H,254,306)(H,255,285)(H,256,288)(H,257,304)(H,258,315)(H,259,296)(H,260,309)(H,261,293)(H,262,294)(H,263,307)(H,264,295)(H,273,274)(H,275,276)(H,277,278)(H,279,280)(H,281,282)(H,317,318)(H4,215,216,225)(H4,217,218,226)(H4,219,220,227)(H4,221,222,228)(H4,223,224,229)/t114-,115-,116-,117+,122-,123-,124-,125-,126-,127-,128-,129-,130-,131-,132-,133-,134-,135-,136-,137-,138-,139-,140-,141-,142-,143-,144-,145-,146-,147-,148-,149-,150-,160-,161-,162-,163-,164-,165-/m0/s1

InChI Key

PPOZQCRGVKQGCX-XAMSXPGMSA-N

Canonical SMILES

CCC(C)C(C(=O)NC(CCCCN)C(=O)NCC(=O)NC(CCC(=O)O)C(=O)NC(CC1=CC=CC=C1)C(=O)NC(CC(C)C)C(=O)NC(CCCCN)C(=O)NC(C(C)O)C(=O)N2CCCC2C(=O)NC(CCC(=O)O)C(=O)NC(C(C)C)C(=O)NC(CCCNC(=N)N)C(=O)NC(CC3=CC=CC=C3)C(=O)NC(CCCNC(=N)N)C(=O)NC(CC(=O)O)C(=O)NC(C(C)CC)C(=O)NC(CCCCN)C(=O)NC(CC(C)C)C(=O)NC(CCCCN)C(=O)NC(CC(=O)O)C(=O)NC(CC(=O)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(C(C)CC)C(=O)NC(CO)C(=O)NC(C(C)C)C(=O)NC(CCC(=O)N)C(=O)NC(CCCNC(=N)N)C(=O)O)NC(=O)C(CCCCN)NC(=O)C(CO)NC(=O)C(CC4=CC=CC=C4)NC(=O)C(CCC(=O)O)NC(=O)C(CC5=CC=CC=C5)NC(=O)C(CCCNC(=N)N)NC(=O)C(CC(C)C)NC(=O)C(CCCCN)NC(=O)C(CC(C)C)NC(=O)CN

1. The human cathelicidin LL-37 modulates the activities of the P2X7 receptor in a structure-dependent manner

Linda Tomasinsig, et al. J Biol Chem. 2008 Nov 7;283(45):30471-81. doi: 10.1074/jbc.M802185200. Epub 2008 Sep 2.

Extracellular ATP, released at sites of inflammation or tissue damage, activates the P2X(7) receptor, which in turn triggers a range of responses also including cell proliferation. In this study the ability of the human cathelicidin LL-37 to stimulate fibroblast growth was inhibited by commonly used P2X(7) blockers. We investigated the structural requirements of the growth-promoting activity of LL-37 and found that it did not depend on helix sense (the all-d analog was active) but did require a strong helix-forming propensity in aqueous solution (a scrambled analog and primate LL-37 orthologs devoid of this property were inactive). The involvement of P2X(7) was analyzed using P2X(7)-expressing HEK293 cells. LL-37 induced proliferation of these cells, triggered Ca(2+) influx, promoted ethidium bromide uptake, and synergized with benzoyl ATP to enhance the pore and channel functions of P2X(7). The activity of LL-37 had an absolute requirement for P2X(7) expression as it was blocked by the P2X(7) inhibitor KN-62, was absent in cells lacking P2X(7), and was restored by P2X(7) transfection. Of particular interest, LL-37 led to pore-forming activity in cells expressing a truncated P2X(7) receptor unable to generate the non-selective pore typical of the full-length receptor. Our results indicate that P2X(7) is involved in the proliferative cell response to LL-37 and that the structural/aggregational properties of LL-37 determine its capacity to modulate the activation state of P2X(7).

2. LL-37 induces polymerization and bundling of actin and affects actin structure

Asaf Sol, Edna Blotnick, Gilad Bachrach, Andras Muhlrad PLoS One. 2012;7(11):e50078. doi: 10.1371/journal.pone.0050078. Epub 2012 Nov 26.

Actin exists as a monomer (G-actin) which can be polymerized to filaments) F-actin) that under the influence of actin-binding proteins and polycations bundle and contribute to the formation of the cytoskeleton. Bundled actin from lysed cells increases the viscosity of sputum in lungs of cystic fibrosis patients. The human host defense peptide LL-37 was previously shown to induce actin bundling and was thus hypothesized to contribute to the pathogenicity of this disease. In this work, interactions between actin and the cationic LL-37 were studied by optical, proteolytic and surface plasmon resonance methods and compared to those obtained with scrambled LL-37 and with the cationic protein lysozyme. We show that LL-37 binds strongly to CaATP-G-actin while scrambled LL-37 does not. While LL-37, at superstoichiometric LL-37/actin concentrations polymerizes MgATP-G-actin, at lower non-polymerizing concentrations LL-37 inhibits actin polymerization by MgCl(2) or NaCl. LL-37 bundles Mg-F-actin filaments both at low and physiological ionic strength when in equimolar or higher concentrations than those of actin. The LL-37 induced bundles are significantly less sensitive to increase in ionic strength than those induced by scrambled LL-37 and lysozyme. LL-37 in concentrations lower than those needed for actin polymerization or bundling, accelerates cleavage of both monomer and polymer actin by subtilisin. Our results indicate that the LL-37-actin interaction is partially electrostatic and partially hydrophobic and that a specific actin binding sequence in the peptide is responsible for the hydrophobic interaction. LL-37-induced bundles, which may contribute to the accumulation of sputum in cystic fibrosis, are dissociated very efficiently by DNase-1 and also by cofilin.

3. The human Cathelicidin LL-37 induces MUC5AC mucin production by airway epithelial cells via TACE-TGF-α-EGFR pathway

Yuke Zhang, Maoxiang Zhu, Zhihua Yang, Xiujie Pan, Yuanyuan Jiang, Congcong Sun, Qin Wang, Wei Xiao Exp Lung Res. 2014 Sep;40(7):333-42. doi: 10.3109/01902148.2014.926434. Epub 2014 Jun 5.

Aim: To investigate the mechanism for LL-37 inducing MUC5AC mucin production in airway epithelial cells. Materials and methods: The airway epithelial NCI-H292 cells were stimulated with various concentrations of LL-37 synthetic peptide and scrambled LL-37 (sLL-37) synthetic peptide ranged from 2.5 to 10 μg/mL. The effects of LL-37 and sLL-37 on TNF-α-converting enzyme (TACE) and EGFR activation and MUC5AC mucin production were evaluated by fluorescence resonance energy transfer (FRET) assay, Western blotting and ELISA respectively. Furthermore, we measured changes of transforming growth factor-alpha (TGF-α) in culture supernatants. A serious of inhibitors including TACE inhibitor TAPI-1, EGFR inhibitor AG1478, EGFR-neutralizing antibody, TGF-α-neutralizing antibody, amphiregulin (AR)-neutralizing antibody, and heparin binding-epidermal growth factor (HB-EGF)-neutralizing antibody were used to block the signaling pathway. Human serum and FBS were also used to investigate the effects of serum on LL-37-induced MUC5AC mucin production. Results: LL-37 induced TACE and EGFR activation, as well as TGF-α and MUC5AC mucin production by NCI-H292 cells in a dose-dependent manner. EGFR-neutralizing antibody and AG1478 inhibited LL-37-induced EGFR activation and subsequent MUC5AC mucin production, whereas TGF-α-neutralizing antibody increased LL-37-induced TGF-α production. TAPI-1 inhibited LL-37-induced TGF-α production, EGFR activation and subsequent MUC5AC mucin production, whereas TGF-α-neutralizing antibody, but not AR- or HB-EGF-neutralizing antibody, inhibited LL-37-induced EGFR activation and subsequent MUC5AC mucin production in NCI-H292 cells. The sLL-37 had no effect on TACE and EGFR activation and MUC5AC mucin production. Additionally, Human serum, rather than FBS, inhibited LL-37-induced MUC5AC mucin production. Conclusions: LL-37 induces MUC5AC mucin production by airway epithelial cells via TACE-TGF-α-EGFR pathway.