HuwentoxinIV (HwTx-IV) isaneurotoxinthatwasoriginallyisolatedfromHaplopelmaschmidti(Chinesebirdspider).Thislethalneurotoxinactsselectivelyon tetrodotoxin-sensitive(TTX-S)voltage-gatedsodiumchannels,withanIC50 of30nMinratDRGneurons.Itpreferentiallyinhibitsneuronal voltage-gatedsodiumchannelsubtypehNav1.7 (SCN9A,IC50 is26nM), rNav1.2 (SCN2A,IC50 is150nM),and rNav1.3 (SCN3A,IC50 is338nM),comparedwithmusclesubtypesrNav1.4(SCN4A)andhNav1.5(SCN5A)(IC50 is>10µM).HuwentoxinIV inhibitstheactivationofsodiumchannelsbytrappingthevoltagesensorofdomainIIofthesite4intheinward,closedconfiguration.Cy5-HuwentoxinIVisafluorescentlytaggedversionofHuwentoxinIV.
Description:
AAsequence: Glu-Cys2-Leu-Glu-Ile-Phe-Lys-Ala-Cys9-Asn-Pro-Ser-Asn-Asp-Gln-Cys16-Cys17-Lys-Ser-Ser-Lys-Leu-Val-Cys24-Ser-Arg-Lys-Thr-Arg-Trp-Cys31-Lys-Tyr-Gln-Ile-NH2
Disulfidebonds: Cys2-Cys17,Cys9-Cys24 andCys16-Cys31
Length(aa): 35
FormulaofHwTx-IV: C174H277N51O52S6
MolecularWeightofHwTx-IV: 4107.20Da
Appearance:darklyophilizedsolid
Solubility: waterandsalinebuffer
CASnumber:
Source: Synthetic
Purityrate: >95%
Cy5:λex646nm,λem662nm
Stoichiometry:1:1
Reference:
Analysisofthestructuralandmolecularbasisofvoltage-sensitivesodiumchannelinhibitionbythespidertoxin,Huwentoxin-IV(μ-TRTX-Hh2a)
Voltage-gatedsodiumchannels(VGSCs)areessentialtothenormalfunctionofthevertebratenervoussystem.AberrantfunctionofVGSCsunderliesavarietyofdisorders,includingepilepsy,arrhythmia,andpain.Alargenumberofanimaltoxinstargettheseionchannelsandmayhavesignificanttherapeuticpotential.Mostofthesetoxins,however,havenotbeencharacterizedindetail.Here,bycombiningpatchclampelectrophysiologyandrADIoligandbindingstudieswithpeptidemutagenesis,NMRstructuredetermination,andmolecularmodeling,wehaverevealedkeymoleculardeterminantsoftheinteractionbetweenthetarantulatoxinhuwentoxin-IVandtwoVGSCisoforms,Nav1.7andNav1.2.Ninehuwentoxin-IVresidues(F6A,P11A,D14A,L22A,S25A,W30A,K32A,Y33A,andI35A)wereimportantforblockofNav1.7andNav1.2.Importantly,moleculardynamicssimulationsandNMRstudiesindicatedthatfoldingwasnormalforseveralkeymutants,suggestingthattheseaminoacidsprobablymakespecificinteractionswithsodiumchannelresidues.Additionally,weidentifiedseveralaminoacids(F6A,K18A,R26A,andK27A)thatareinvolvedinisoform-specificVGSCinteractions.Ourstructuralandfunctionaldatawereusedtomodelthedockingofhuwentoxin-IVintothedomainIIvoltagesensorofNav1.7.ThemodelpredictsthatahydrophobicpatchcomposedofTrp-30andPhe-6,alongwiththebasicLys-32residue,docksintoagrooveformedbytheNav1.7S1-S2andS3-S4loops.Theseresultsprovidenewinsightintothestructuralandmolecularbasisofsodiumchannelblockbyhuwentoxin-IVandmayprovideabasisfortherationaldesignoftoxin-basedpeptideswithimprovedVGSCpotencyand/orselectivity.
MinassianNA.,etal.(2013)Analysisofthestructuralandmolecularbasisofvoltage-sensitivesodiumchannelinhibitionbythespidertoxin,Huwentoxin-IV(μ-TRTX-Hh2a). JBC. PMID: 23760503
Commonmoleculardeterminantsoftarantulahuwentoxin-IVinhibitionofNa+channelvoltagesensorsindomainsIIandIV
ThevoltagesensorsofdomainsIIandIVofsodiumchannelsareimportantdeterminantsofactivationandinactivation,respectively.AnimaltoxinsthatalterelectrophysiologicalexcitABIlityofmusclesandneuronsoftenmodifysodiumchannelactivationbyselectivelyinteractingwithdomainIIandinactivationbyselectivelyinteractingwithdomainIV.Thissuggeststhattheremaybesubstantialdifferencesbetweenthetoxin-bindingsitesinthesetwoimportantdomains.Hereweexploretheabilityofthetarantulahuwentoxin-IV(HWTX-IV)toinhibittheactivityofthedomainIIandIVvoltagesensors.HWTX-IVisspecificfordomainII,andweidentifyfiveresiduesintheS1-S2(Glu-753)andS3-S4(Glu-811,Leu-814,Asp-816,andGlu-818)regionsofdomainIIthatarecrucialforinhibitionofactivationbyHWTX-IV.ThesedataindicatethatasingleresidueintheS3-S4linker(Glu-818inhNav1.7)iscrucialforallowingHWTX-IVtointeractwiththeotherkeyresiduesandtrapthevoltagesensorintheclosedconfiguration.MutagenesisanalysisindicatesthatthefivecorrespondingresiduesindomainIVareallcriticalforendowingHWTX-IVwiththeabilitytoinhibitfastinactivation.Ourdatasuggestthatthetoxin-bindingmotifindomainIIisconservedindomainIV.Increasingourunderstandingofthemoleculardeterminantsoftoxininteractionswithvoltage-gatedsodiumchannelsmaypermitdevelopmentofenhancedisoform-specificvoltage-gatingmodifiers.
Xiao,Y., etal.(2011)Commonmoleculardeterminantsoftarantulahuwentoxin-IVinhibitionofNa+channelvoltagesensorsindomainsIIandIV, JBC. PMID: 21659528
ThetarantulatoxinsProTx-IIandhuwentoxin-IVdifferentiallyinteractwithhumanNav1.7voltagesensorstoinhibitchannelactivationandinactivation
Thevoltage-gatedsodiumchannelNa(v)1.7playsacrucialroleinpain,anddrugsthatinhibithNa(v)1.7mayhavetremendoustherapeuticpotential.ProTx-IIandhuwentoxin-IV(HWTX-IV),cystineknotpeptidesfromtarantulavenoms,preferentiallyblockhNa(v)1.7.Understandingtheinteractionsofthesetoxinswithsodiumchannelscouldaidthedevelopmentofnovelpaintherapeutics.WhereasbothProTx-IIandHWTX-IVhavebeenproposedtopreferentiallyblockhNa(v)1.7activationbytrappingthedomainIIvoltage-sensorintherestingconfiguration,weshowthatspecificresiduesinthevoltage-sensorpaddleofdomainIIplaysubstantiallydifferentrolesindeterminingtheaffinitiesofthesetoxinstohNa(v)1.7.ThemutationE818CincreasesProTx-II‘sandHWTX-IV‘sIC(50)forblockofhNa(v)1.7currentsby4-and400-fold,respectively.Incontrast,themutationF813GdecreasesProTx-IIaffinityby9-foldbuthasnoeffectonHWTX-IVaffinity.ItisnoteworthythatwealsoshowthatProTx-II,butnotHWTX-IV,preferentiallyinteractswithhNa(v)1.7toimpedefastinactivationbytrappingthedomainIVvoltage-sensorintherestingconfiguration.MutationsE1589QandT1590KindomainIVeachdecreasedProTx-II’sIC(50)forimpairmentoffastinactivationby~6-fold.IncontrastmutationsD1586AandF1592Aindomain-IVincreasedProTx-II’sIC(50)forimpairmentoffastinactivationby~4-fold.OurresultsshowthatwhereasProTx-IIandHWTX-IVbindingdeterminantsondomain-IImayoverlap,domainIIplaysamuchmorecrucialroleforHWTX-IV,andcontrarytowhathasbeenproposedtobeaguidingprincipleofsodiumchannelpharmacology,moleculesdonothavetoexclusivelytargetthedomainIVvoltage-sensortoinfluencesodiumchannelinactivation.
Xiao,Y., etal.(2010)ThetarantulatoxinsProTx-IIandhuwentoxin-IVdifferentiallyinteractwithhumanNav1.7voltagesensorstoinhibitchannelactivationandinactivation, MolPharmacol. PMID: 20855463
Mechanismofactionoftwoinsecttoxinshuwentoxin-IIIandhainantoxin-VIonvoltage-gatedsodiumchannels
SelenocosmiahuwenaandSelenocosmiahainanaaretwotarantulaspeciesfoundinsouthernChina.Theirvenomscontainabundantpeptidetoxins.Twonewneurotoxicpeptides,huwentoxin-III(HWTX-III)andhainantoxin-VI(HNTX-VI),wereobtainedfromthevenomusingion-exchangechromatographyandreverse-phasehighperformanceliquidchromatography(RP-HPLC).ThemechanismofactionofHWTX-IIIandHNTX-VIoninsectneuronalvoltage-gatedsodiumchannels(VGSCs)wasstudiedviawhole-cellpatchclamptechniques.Inafashionsimilartodelta-atracotoxins,HNTX-VIcaninduceaslowdownofcurrentinactivationoftheVGSCandreductioninthepeakofNa+currentincockroachdorsalunpairedmedian(DUM)neurons.Meanwhile,10micromol/LHNTX-IVcausedapositiveshiftofsteady-stateinactivationofsodiumchannel.HWTX-IIIinhibitedVGSCsonDUMneurons(concentrationoftoxinathalf-maximalinhibition(IC(50))approximately1.106micromol/L)inawaymuchsimilartotetrodotoxin(TTX).HWTX-IIIhadnoeffectonthekineticsofactivationandinactivation.Theshiftinthesteady-stateinactivationcurvewasdistinctfromotherdepressantspidertoxins.ThediverseeffectandthemechanismofactionofthetwoinsecttoxinsillustratethediverseBIOLOGicalactivitiesofspidertoxinsandprovideafreshtheoreticalfoundationtodesignanddevelopnovelinsecticides.
WangRL, etal.(2010)Mechanismofactionoftwoinsecttoxinshuwentoxin-IIIandhainantoxin-VIonvoltage-gatedsodiumchannels. PMID: 20506577
Tarantulahuwentoxin-IVinhibitsneuronalsodiumchannelsbybindingtoreceptorsite4andtrappingthedomainiivoltagesensorintheclosedconfiguration
Peptidetoxinswithhighaffinity,divergentpharmacologicalfunctions,andisoform-specificselectivityarepowerfultoolsforinvestigatingthestructure-functionrelationshipsofvoltage-gatedsodiumchannels(VGSCs).Althoughanumberofinterestinginhibitorshavebeenreportedfromtarantulavenoms,littleisknownaboutthemechanismfortheirinteractionwithVGSCs.Weshowthathuwentoxin-IV(HWTX-IV),a35-residuepeptidefromtarantulaOrnithoctonushuwenavenom,preferentiallyinhibitsneuronalVGSCsubtypesrNav1.2,rNav1.3,andhNav1.7comparedwithmusclesubtypesrNav1.4andhNav1.5.OfthefiveVGSCsexamined,hNav1.7wasmostsensitivetoHWTX-IV(IC(50)approximately26nM).Followingapplicationof1micromHWTX-IV,hNav1.7currentscouldonlybeelicitedwithextremedepolarizations(>+100mV).RecoveryofhNav1.7channelsfromHWTX-IVinhibitioncouldbeinducedbyextremedepolarizationsormoderatedepolarizationslastingseveralminutes.Site-directedmutagenesisanalysisindicatedthatthetoxindockedatneurotoxinreceptorsite4locatedattheextracellularS3-S4linkerofdomainII.MutationsE818QandD816NinhNav1.7decreasedtoxinaffinityforhNav1.7byapproximately300-fold,whereasthereversemutationsinrNav1.4(N655D/Q657E)andthecorrespondingmutationsinhNav1.5(R812D/S814E)greatlyincreasedthesensitivityofthemuscleVGSCstoHWTX-IV.Ourdataidentifyanovelmechanismforsodiumchannelinhibitionbytarantulatoxinsinvolvingbindingtoneurotoxinreceptorsite4.Incontrasttoscorpionbeta-toxinsthattraptheIIS4voltagesensorinanoutwardconfiguration,weproposethatHWTX-IVtrapsthevoltagesensorofdomainIIintheinward,closedconfiguration.
Xiao,Y., etal.(2008)Tarantulahuwentoxin-IVinhibitsneuronalsodiumchannelsbybindingtoreceptorsite4andtrappingthedomainiivoltagesensorintheclosedconfiguration, JBC. PMID: 18628201
Functionandsolutionstructureofhuwentoxin-IV,apotentneuronaltetrodotoxin(TTX)-sensitivesodiumchannelantagoNISTfromChinesebirdspiderSelenocosmiahuwena
WehaveisolatedahighlypotentneurotoxinfromthevenomoftheChinesebirdspider,Selenocosmiahuwena.This4.1-kDatoxin,whichhasbeennamedhuwentoxin-IV,contains35residueswiththreedisulfidebridges:Cys-2-Cys-17,Cys-9-Cys-24,andCys-16-Cys-31,assignedbyachemicalstrategyincludingpartialreductionofthetoxinandsequenceanalysisofthemodifiedintermediates.Itspecificallyinhibitstheneuronaltetrodotoxin-sensitive(TTX-S)voltage-gatedsodiumchannelwiththeIC(50)valueof30nminadultratdorsalrootganglionneurons,whilehavingnosignificanteffectonthetetrodotoxin-resistant(TTX-R)voltage-gatedsodiumchannel.ThistoxinseemstobeasiteItoxinaffectingthesodiumchannelthroughamechanismquitesimilartothatofTTX:itsuppressesthepeaksodiumcurrentwithoutalteringtheactivationorinactivationkinetics.Thethree-dimensionalstructureofhuwentoxin-IVhasbeendeterminedbytwo-dimensional(1)HNMRcombinedwithdistantgeometryandsimulatedannealingcalculationbyusing527nuclearOverhausereffectconstraintsand14dihedralconstraints.Theresultingstructureiscomposedofadouble-strandedantiparallelbeta-sheet(Leu-22-Ser-25andTrp-30-Tyr-33)andfourturns(Glu-4-Lys-7,Pro-11-Asp-14,Lys-18-Lys-21andArg-26-Arg-29)andbelongstotheinhibitorcystineknotstructuralfamily.Aftercomparisonwithothertoxinspurifiedfromthesamespecies,weareconvincedthatthepositivelychargedresiduesofloopIV(residues25-29),especiallyresidueArg-26,mustbecrucialtoitsbindingtotheneuronaltetrodotoxin-sensitivevoltage-gatedsodiumchannel.
Peng,K., etal.(2002)Functionandsolutionstructureofhuwentoxin-IV,apotentneuronaltetrodotoxin(TTX)-sensitivesodiumchannelantagonistfromChinesebirdspiderSelenocosmiahuwena, JBiolChem.PMID: 12228241
Smartox"scitation:Anaturalpointmutationchangesbothtargetselectivityandmechanismofactionofseaanemonetoxins
APETx3,anovelpeptideisolatedfromtheseaanemoneAnthopleuraelegantissima,isanaturallyoccurringmutantfromAPETx1,onlydifferingbyaThrtoProsubstitutionatposition3.APETx1isbelievedtobeaselectivemodulatorofhumanether-á-go-gorelatedgene(hERG)potassiumchannelswithaK(d)of34nM.Inthisstudy,APETx1,2,and3havebeensubjectedtoanelectrophysiologicalscreeningonawiderangeof24ionchannelsexpressedinXenopuslaevisoocytes:10clonedvoltage-gatedsodiumchannels(Na(V)1.2-Na(V)1.8,theinsectchannelsDmNa(V)1,BgNa(V)1-1a,andthearachnidchannelVdNa(V)1)and14clonedvoltage-gatedpotassiumchannels(K(V)1.1-K(V)1.6,K(V)2.1,K(V)3.1,K(V)4.2,K(V)4.3,K(V)7.2,K(V)7.4,hERG,andtheinsectchannelShakerIR).Surprisingly,theThr3ProsubstitutionresultsinacompleteabolishmentofAPETx3modulationonhERGchannelsandprovidesthistoxintheabilitytobecomeapotent(EC(50)276nM)modulatorofvoltage-gatedsodiumchannels(Na(V)s)becauseitslowsdowntheinactivationofmammalianandinsectNa(V)channels.OurstudyalsoshowsthatthehomologoustoxinsAPETx1andAPETx2displaypromiscuouspropertiessincetheyarealsocapableofrecognizingNa(V)channelswithIC(50)valuesof31nMand114nM,respectively,causinganinhibitionofthesodiumconductancewithoutaffectingtheinactivation.Ourresultsprovidenewinsightsinkeyresiduesthatallowtheseseaanemonetoxinstorecognizedistinctionchannelswithsimilarpotencybutwithdifferentmodulatoryeffects.FurThermore,wedescribeforthefirsttimethetargetpromiscuityofafamilyofseaanemonetoxinsthusfarbelievedtobehighlyselective.
PeigneurS, etal. (2012)Anaturalpointmutationchangesbothtargetselectivityandmechanismofactionofseaanemonetoxins. FASEBJ. PMID: 22972919
Smartox Biotechnolgy的多肽毒素产品如下：
1. 作用于钠离子通道(Sodium channel)的毒素
Toxin name | Catalog # | Target |
Phrixotoxin-3 | 13PHX003 | Selective blocker of Nav1.2 |
µ-conotoxin GIIIB | CON020 | Selective blocker of Nav1.4 |
µ-conotoxin CnIIIC | CON021 | Selective blocker of Nav1.4 |
μ-conotoxin PIIIA | 08CON006 | Selective blocker of Nav1.4 |
Jingzhaotoxin-III | 12JZH003 | Selective blocker of Nav1.5 |
ProTx-II | 07PTX002 | Selective blocker of Nav1.7 |
ProTx-II Biotin | 12PTB002 | Selective blocker of Nav1.7 |
ProTx-I | 12PTX001 | Blocker of Nav1.8, Nav1.2, Nav1.5, Nav1.7 |
Huwentoxin-I | 07HWT001 | Blocker of TTX-S |
Huwentoxin-IV | 08HWT002 | Blocker of TTX-S |
Hainantoxin-III | 13HTX003 | Blocker of TTX-S |
Hainantoxin-IV | 12HTX001 | Blocker of TTX-S |
GsAF-I | 12GSF001 | Blocker of TTX-S |
GsAF-II | 12GSF002 | Blocker of TTX-S |
2. 作用于钾离子通道(Potassium channel)的毒素
Toxin name | Catalog # | Target |
KCa channels | ||
Apamin 蜜蜂神经毒素 | 08APA001 | SK1, SK2, SK3 |
Charybdotoxin 蝎毒素 | 11CHA001 | KCa1.1, KCa3.1 - Kv1.2, Kv1.3, Kv1.6 |
Iberiotoxin | 12IBX001 | KCa1.1 |
Leiurotoxin 1 (Scyllatoxin) | 10LEI001 | SK1, SK2, SK3 |
Tamapin | 10TAM001 | SK1, SK2, SK3 |
Kaliotoxin-1 | 08KTX002 | BK, Kv1.1, Kv1.2, Kv1.3 |
Kv channels | ||
ShK | 08SHK001 | Kv1.3, Kv1.1, Kv1.4, Kv1.6 |
TMR-ShK | SAT001 | Kv1.3, Kv1.1 |
Margatoxin | 08MAG001 | Kv1.3 |
(Dap22)-ShK | 13SHD001 | Kv1.3 |
ADWX-1 | 13ADW001 | Kv1.3 |
HsTx1 | 08NEU001 | Kv1.3, Kv1.2 |
Agitoxin-2 | 13AGI002 | Kv1.3, Kv1.1 |
Maurotoxin | 08MAR001 | Kv1.2, KCa3.1 |
Guangxitoxin 1E | 11GUA002 | Kv2.1, Kv2.2 |
Stromatoxin 1 NEW | SCT01 | Kv2.1, Kv2.2 |
Kaliotoxin-1 | 08KTX002 | BK, Kv1.1, Kv1.2, Kv1.3 |
Charybdotoxin | 11CHA001 | KCa1.1, KCa3.1 - Kv1.2, Kv1.3, Kv1.6 |
Phrixotoxin-2 | PHX002 | Kv4.2, Kv4.3 |
AmmTx3 NEW | AMX001 | A-type potassium channels |
Inwardly rectifying potassium channels | ||
TertiapinQ | 08TER001 | Kir1.1, Kir3.1/3.4, Kir3.1/3.2-KCa1.1 |
hERG/Kv11.1 | ||
BeKm-1 | 13BEK001 | ERG1 |
3. 作用于钙离子通道(Calcium channel)的毒素
Toxin name | Catalog # | Target |
High voltage-gated Ca2+ channels | ||
ω-agatoxin IVA | 11AGA001 | P/Qtype |
ω-Conotoxin MVIIC | 08CON002 | P/Qtype, N-type |
ω-Conotoxin MVIIA | 08CON001 | N-type |
ω-Conotoxin GVIA | 08CON003 | N-type |
ω-Conotoxin SO3 | 08CON013 | N-type |
Huwentoxin I | 07HWT001 | N-type |
ProTx-II | 07PTX002 | T-type, L-type |
Intermediate voltage-gated Ca2+ channels | ||
SNX482 | 08SNX002 | R-type |
Low voltage-gated Ca2+ channels | ||
ProTx-I | 12PTX001 | T-type |
ProTx-II | 07PTX002 | T-type, L-type |
Ryanodine receptors | ||
Maurocalcine | 07PAU001 | Ryr1 |
4. 作用于氯离子通道(Chloride channel)的毒素
Toxin name | Catalog # | Target |
Chlorotoxin | 08CHL001 | Blocker of small conductance Cl- channels |
GaTx1 | 13GTX001 | Selective blocker of CFTR channel |
GaTx2 | 10GTX002 | Selective blocker of ClC-2 channel |
5. 作用于乙酰胆碱受体(Acetylcholine receptor)的毒素
Toxin name | Catalog # | Target |
α-conotoxin PeIA | 13CON017 | α9α10, α3β2 subunits |
α-Conotoxin PrXA | 13CON016 | α1/β1/ε/δ, α1/β1/γ/δ subunits |
Waglerin-1 | 12WAG001 | MusclenAChR |
α-conotoxin MI | 08CON012 | α1/δsubunits |
α-conotoxin GI | 08CON005 | α/δsite |
α-conotoxin IMI | 08CON011 | α7 homomeric nAChR |
α-conotoxin GID | CON019 | Blocker of α3β2, α7 and α4β2 nAChRs |
6. 含N-甲基-D-天冬氨酸NR2B
(NMDA, NR2B containing N-methyl-D-aspartate)
Conantokin-G
选择性、特异性抑制含NR2B的NMDAR。Conantokin-G能剂量依赖性抑制Ca2+内流，抑制NMDA诱导的兴奋性中毒效应。研究表明，在小鼠皮层神经元，Conantokin-G阻滞NMDA引发的电流信号的IC50值为480 nM。
7. 作用于酸敏感离子通道(ASIC channel, Acid-Sensing Ion Channel)的毒素
Toxin name | Catalog # | Target |
APETx2 | 07APE002 | Selective blocker of ASIC3 |
Psalmotoxin1/PcTx1 | 13PCT001 | Selective blocker of ASIC1a |
Ugr9-1 | 13UGR001 | Blocker of ASIC3 |
8. 作用于瞬时受体电位(TRP channel, transient receptor potential)的毒素
Toxin name | Catalog # | Target |
GsMTx4 | 08GSM001 | TRPC, TRPA |
Vanillotoxin3 | 10VAN003 | Activator of TRPV1 |
ProTx-I | 12PTX001 | Antagonist of TRPA1 |
9. 作用于嘌呤能通道(Purinergic channel)的毒素
Purotoxin-1
选择性抑制P2X3受体。100 nM Purotoxin-1 (PT-1)选择性抑制P2X3受体通道，在大鼠DRG神经元上，使用膜片钳实验表明：PT-1对电压门控通道和TRPV1均无抑制效应。10 µM ATP和100 µM α,β Methylene-ATP浓度下Purotoxin-1对P2X3受体有选择性作用，在该ATP浓度下Purotoxin-1对P2X2和杂化二聚体P2X2/3并无激动作用。Purotoxin-1对疼痛的潜在治疗作用。
10. 作用于其它膜受体通道(Others)的毒素
Smartox Biotechnology还提供其他类型的膜受体抑制剂：
Toxin name | Catalog # | Target |
Morphiceptin | 011CAS001 | Agonist of µ-opoid receptors |
Lys-conopressin G | 11CON14 | Vasopressin-like peptide |
GsMTx4 | 08GSM001 | Mechano sensitive ion channels |
Obtustatin | 10OBT001 | Blocks the binding of α1β1 integrin to collagen IV |
Rho-Conotoxin TIA | CON022 | Blocks α1-adrenergic receptor |
公司简介
Smartox Biotechnology是全球唯一一家专门生产动物毒液多肽毒素，用于细胞离子通道功能研究的生物医药公司。多肽毒素在生物制药领域具有重要的使用价值。
Smartox Biotechnology于2009年由来自Grenoble神经科学研究所(Grenoble Institute of Neuroscience)的Michel De Waard博士创立。Smartox Biotechnology专门研究动物毒液，制作合成多种毒液中的多肽成分（常称为毒素）。De Waard博士研究离子通道与毒素多肽的关系，尤其是鉴定、开发毒素多肽作为治疗性分子或细胞穿透肽(cell penetrating peptides, CPP)。其研究团队在毒液分离，药理性活性肽鉴定、富半胱氨酸肽定性、制作和优化等方面具有独特、丰富的经验。2010年，Smartox Biotechnolgy被法国研究部(Ministry of Research)授予“新兴企业OSEO奖(OSEO prize for emerging businesses)”。
总之，Smartox Biotechnolgy提供一系列高质量、具开创价值的多肽毒素。这些化合物在离子通道 研究中具有高的亲和性和选择性，是相应领域科学研究理想的生物毒素提供商和贴心的合作伙伴。
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