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Defensin 5 (human)

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

Defensin 5 (human), a key regulator of gut microbiota homeostasis, shows microbicidal activity against bacteria, fungi, and viruses and is released by Paneth cells in the small intestine. The reduction or loss of HD 5 release from intestinal mucosa is associated with susceptibility to enteric pathogens, changes in microbial composition, and disruption of intestinal immune homeostasis. As a biomarker, it can be used to distinguish between ulcerative colitis (low levels of HD 5) or Crohn's colitis (high levels of HD 5).

Category

Functional Peptides

Catalog number

BAT-014814

Molecular Formula

C144H238N50O45S6

Molecular Weight

3582.18

Specification
Reference Reading

IUPAC Name

(2S)-2-[[(1R,4S,7S,13S,16R,19S,22S,25S,28S,31S,34S,37S,43S,46R,49S,52S,55S,61S,64S,67S,70S,73S,76R,79R,84R,87S)-84-[[(2S,3R)-2-[[(2S)-2-aminopropanoyl]amino]-3-hydroxybutanoyl]amino]-52-[(2S)-butan-2-yl]-4,13,25,61,70-pentakis(3-carbamimidamidopropyl)-28,49-bis(2-carboxyethyl)-7,22-bis[(1R)-1-hydroxyethyl]-31,37,55-tris(hydroxymethyl)-67,87-bis[(4-hydroxyphenyl)methyl]-19-methyl-34,64,73-tris(2-methylpropyl)-2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,85,88-octacosaoxo-43-propan-2-yl-81,82,91,92,95,96-hexathia-3,6,9,12,15,18,21,24,27,30,33,36,39,42,45,48,51,54,57,60,63,66,69,72,75,78,86,89-octacosazatricyclo[44.43.4.416,76]heptanonacontane-79-carbonyl]amino]-5-carbamimidamidopentanoic acid

Synonyms

Defensin HD 5; H-Ala-Thr-Cys-Tyr-Cys-Arg-Thr-Gly-Arg-Cys-Ala-Thr-Arg-Glu-Ser-Leu-Ser-Gly-Val-Cys-Glu-Ile-Ser-Gly-Arg-Leu-Tyr-Arg-Leu-Cys-Cys-Arg-OH (Disulfide bridge: Cys3-Cys31, Cys5-Cys20, Cys10-Cys30, air oxidized); L-alanyl-L-threonyl-L-cysteinyl-L-tyrosyl-L-cysteinyl-L-arginyl-L-threonyl-glycyl-L-arginyl-L-cysteinyl-L-alanyl-L-threonyl-L-arginyl-L-alpha-glutamyl-L-seryl-L-leucyl-L-seryl-glycyl-L-valyl-L-cysteinyl-L-alpha-glutamyl-L-isoleucyl-L-seryl-glycyl-L-arginyl-L-leucyl-L-tyrosyl-L-arginyl-L-leucyl-L-cysteinyl-L-cysteinyl-L-arginine (3->31),(5->20),(10->30)-tris(disulfide); Human defensin-5 (HD 5)

Appearance

White Powder

Purity

≥95%

Density

1.6±0.1 g/cm3

Sequence

ATCYCRTGRCATRESLSGVCEISGRLYRLCCR (Disulfide bridge: Cys3-Cys31, Cys5-Cys20, Cys10-Cys30)

Storage

Store at -20°C

Solubility

Soluble in Water

InChI

InChI=1S/C144H238N50O45S6/c1-16-68(10)106-135(235)183-92(56-196)113(213)164-52-100(203)168-78(23-17-41-158-139(146)147)114(214)176-86(47-64(2)3)121(221)179-89(50-74-29-33-76(201)34-30-74)124(224)170-80(25-19-43-160-141(150)151)117(217)177-88(49-66(6)7)123(223)185-97-61-243-240-58-94-127(227)167-70(12)111(211)193-109(73(15)200)136(236)174-81(26-20-44-161-142(152)153)116(216)172-83(37-39-103(206)207)118(218)182-93(57-197)126(226)178-87(48-65(4)5)122(222)181-91(55-195)112(212)165-54-102(205)190-105(67(8)9)134(234)188-98(129(229)173-84(120(220)191-106)38-40-104(208)209)62-244-241-59-95(128(228)171-82(27-21-45-162-143(154)155)119(219)194-107(71(13)198)133(233)166-53-101(204)169-79(115(215)184-94)24-18-42-159-140(148)149)186-125(225)90(51-75-31-35-77(202)36-32-75)180-131(231)99(189-137(237)108(72(14)199)192-110(210)69(11)145)63-245-242-60-96(187-132(97)232)130(230)175-85(138(238)239)28-22-46-163-144(156)157/h29-36,64-73,78-99,105-109,195-202H,16-28,37-63,145H2,1-15H3,(H,164,213)(H,165,212)(H,166,233)(H,167,227)(H,168,203)(H,169,204)(H,170,224)(H,171,228)(H,172,216)(H,173,229)(H,174,236)(H,175,230)(H,176,214)(H,177,217)(H,178,226)(H,179,221)(H,180,231)(H,181,222)(H,182,218)(H,183,235)(H,184,215)(H,185,223)(H,186,225)(H,187,232)(H,188,234)(H,189,237)(H,190,205)(H,191,220)(H,192,210)(H,193,211)(H,194,219)(H,206,207)(H,208,209)(H,238,239)(H4,146,147,158)(H4,148,149,159)(H4,150,151,160)(H4,152,153,161)(H4,154,155,162)(H4,156,157,163)/t68-,69-,70-,71+,72+,73+,78-,79-,80-,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,91-,92-,93-,94-,95-,96-,97-,98-,99-,105-,106-,107-,108-,109-/m0/s1

InChI Key

XOGQESQUFLMQCZ-JAIHJDDCSA-N

Canonical SMILES

CCC(C)C1C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC2CSSCC3C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(CSSCC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)N3)CCCNC(=N)N)C(C)O)CCCNC(=N)N)NC(=O)C(NC(=O)C(CSSCC(NC2=O)C(=O)NC(CCCNC(=N)N)C(=O)O)NC(=O)C(C(C)O)NC(=O)C(C)N)CC4=CC=C(C=C4)O)C(=O)NC(C(=O)N1)CCC(=O)O)C(C)C)CO)CC(C)C)CO)CCC(=O)O)CCCNC(=N)N)C(C)O)C)CC(C)C)CCCNC(=N)N)CC5=CC=C(C=C5)O)CC(C)C)CCCNC(=N)N)CO

1. Vibrio cholerae senses human enteric α-defensin 5 through a CarSR two-component system to promote bacterial pathogenicity

Yutao Liu, Tingting Xu, Qian Wang, Junxi Huang, Yangfei Zhu, Xingmei Liu, Ruiying Liu, Bin Yang, Kai Zhou Commun Biol. 2022 Jun 8;5(1):559. doi: 10.1038/s42003-022-03525-3.

Vibrio cholerae (V. cholerae) is an aquatic bacterium responsible for acute and fatal cholera outbreaks worldwide. When V. cholerae is ingested, the bacteria colonize the epithelium of the small intestine and stimulate the Paneth cells to produce large amounts of cationic antimicrobial peptides (CAMPs). Human defensin 5 (HD-5) is the most abundant CAMPs in the small intestine. However, the role of the V. cholerae response to HD-5 remains unclear. Here we show that HD-5 significantly upregulates virulence gene expression. Moreover, a two-component system, CarSR (or RstAB), is essential for V. cholerae virulence gene expression in the presence of HD-5. Finally, phosphorylated CarR can directly bind to the promoter region of TcpP, activating transcription of tcpP, which in turn activates downstream virulence genes to promote V. cholerae colonization. In conclusion, this study reveals a virulence-regulating pathway, in which the CarSR two-component regulatory system senses HD-5 to activate virulence genes expression in V. cholerae.

2. Human defensin-inspired discovery of peptidomimetic antibiotics

Gan Luo, Jue Zhang, HanBin Wang, YaQi Sun, BaoLi Cheng, ZhiPeng Xu, Yan Zhang, Hui Li, WuYuan Lu, Elizabeta Nemeth, Tomas Ganz, XiangMing Fang Proc Natl Acad Sci U S A. 2022 Mar 8;119(10):e2117283119. doi: 10.1073/pnas.2117283119. Epub 2022 Mar 1.

SignificanceWe report the development of peptidomimetic antibiotics derived from a natural antimicrobial peptide, human α-defensin 5. By engaging multiple bacterial targets, the lead compound is efficacious in vitro and in vivo against bacteria with highly inducible antibiotic resistance, promising a useful therapeutic agent for the treatment of infections caused by antibiotic-resistant bacteria.

3. Human Peptides α-Defensin-1 and -5 Inhibit Pertussis Toxin

Carolin Kling, Arto T Pulliainen, Holger Barth, Katharina Ernst Toxins (Basel). 2021 Jul 11;13(7):480. doi: 10.3390/toxins13070480.

Bordetella pertussis causes the severe childhood disease whooping cough, by releasing several toxins, including pertussis toxin (PT) as a major virulence factor. PT is an AB5-type toxin, and consists of the enzymatic A-subunit PTS1 and five B-subunits, which facilitate binding to cells and transport of PTS1 into the cytosol. PTS1 ADP-ribosylates α-subunits of inhibitory G-proteins (Gαi) in the cytosol, which leads to disturbed cAMP signaling. Since PT is crucial for causing severe courses of disease, our aim is to identify new inhibitors against PT, to provide starting points for novel therapeutic approaches. Here, we investigated the effect of human antimicrobial peptides of the defensin family on PT. We demonstrated that PTS1 enzyme activity in vitro was inhibited by α-defensin-1 and -5, but not β-defensin-1. The amount of ADP-ribosylated Gαi was significantly reduced in PT-treated cells, in the presence of α-defensin-1 and -5. Moreover, both α-defensins decreased PT-mediated effects on cAMP signaling in the living cell-based interference in the Gαi-mediated signal transduction (iGIST) assay. Taken together, we identified the human peptides α-defensin-1 and -5 as inhibitors of PT activity, suggesting that these human peptides bear potential for developing novel therapeutic strategies against whooping cough.