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蚂蚁淘在线 / 品牌中心 / Smartox / Smartox/Conotoxin GVIA, a selective blocker of Cav2.2 channel/08CON003-00100/0.1mg

Smartox/Conotoxin GVIA, a selective blocker of Cav2.2 channel/08CON003-00100/0.1mg

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￥1060.80
货号：08CON003-00100
浏览量：127
品牌：Smartox
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商品描述

ω-conotoxin-GVIA(omegaconotoxinGVIA)isaconotoxinthathhasbeenisolatedfromthevenomoftheconeConusgeographus. ω-conotoxinGVIA actsatpresynapticmembranes.Itbindsandblocksspecifically voltage-dependentN-typeCa2+channels Cav2.2channel withanED50 of68pM.


Description:

Productcode:08CON003.Categories:Calciumchannels,Highvoltage-gatedCa2+channels.Tags:106375-28-4,Cav2.2,N-type.

AAsequence: H-Cys1-Lys-Ser-Hyp-Gly-Ser-Ser-Cys8-Ser-Hyp-Thr-Ser-Tyr-Asn-Cys15-Cys16-Arg-Ser-Cys19-Asn-Hyp-Tyr-Thr-Lys-Arg-Cys26-Tyr-NH2
Hyp:hydroxyproline
(DisulfidebondsbetweenCys1-Cys16,Cys8-Cys19 andCys15-Cys26)
Length(aa): 27
Formula: C120H182N38O43S6
MolecularWeight: 3036.05Da
Appearance: Whitelyophilizedsolid
Solubility: waterandsalinebuffer
CASnumber: [106375-28-4]Source: Synthetic
Purityrate: >95%

Reference:

Structure-functionrelationshipsofomega-conotoxinGVIA.Synthesis,structure,calciumchannelbinding,andfunctionalassayofalanine-substitutedanalogues

Thestructure-functionrelationshipsoftheN-typecalciumchannelblocker,omega-conotoxinGVIA(GVIA),havebeenelucidatedbystructural,binding&invitro&invivofunctionalstudiesofalanine-substitutedanaloguesofthenativemolecule.Alaninewassubstitutedatallnon-bridgingpositionsinthesequence.Inmostcasesthestructureoftheanaloguesinaqueoussolutionwasshowntobenative-likeby1HNMRspectroscopy.Minorconformationalchangesobservedinsomecaseswerecharacterizedbytwo-dimensionalNMR.ReplacementofLys2&Tyr13withAlacausedreductionsinpotencyofmorethan2ordersofmagnitudeinthreefunctionalassays(sympatheticnervestimulationofratisolatedvasdeferens,rightatrium&mesentericartery)&aratbrainmembranebindingassay.ReplacementofseveralotherresidueswithAla(particularlyArg17,Tyr22&Lys24)resultedinsignificantreductionsinpotency(<100-fold)inthefunctionalassays,butnotthebindingassay.Thepotenciesoftheanalogueswerestronglycorrelatedbetweenthedifferentfunctionalassaysbutnotbetweenthefunctionalassays&thebindingassay.Thus,thephysiologicallyrelevantassaysemployedinthisstudyhaveshownthatthehighaffinityofGVIAfortheN-typecalciumchannelistheresultofinteractionsbetweenthechannelbindingsite&thetoxinatmoresitesthanthepreviouslyidentifiedLys2&Tyr13.

Lew,M.J., etal. (1997)Structure-functionrelationshipsofomega-conotoxinGVIA.Synthesis,structure,calciumchannelbinding,andfunctionalassayofalanine-substitutedanalogues, JBiolChem. PMID: 9115267
CharacteristicsofOmega-conotoxinGVIAandMVIICBindingtoCav2.1andCav2.2ChannelsCapturedbyAnti-Ca2+ChannelPeptideAntibodies
ANewBindingMethod(NBM)wasusedtoinvestigatethecharacteristicsofthespecificbindingof125I-omega-conotoxin(omega-CTX)GVIAand125I-omega-CTXMVIICtoCav2.1andCav2.2channelscapturedfromchickbrainmembranesbyantibodiesagainstB1Nt(apeptidesequenceinCar2.1&Cav2.2channels).TheresultsfortheNBMwereasfollows.(1)TheED50valuesforspecificbindingof125I-omega-CTXGVIA&125I-omega-CTXMVIICtoCav2.1&Cav2.2channelswereabout68&60pM,respectively,&verysimilartothose(87&35pM,respectively)tocrudemembranesfromchickbrain.(2)Thespecific125I-omega-CTXGVIA(100pM)bindingwasinhibitedbyomega-CTXGVIA(0.5nM),dynorphineA(Dyn),gentamicin(Gen),neomycin(Neo)&tobramicin(Tob)(100microMeach),butnotbyomega-agaconotoxin(Aga)IVA,calciseptine,omega-CTXSVIB,omega-CTXMVIIC(0.5nMeach),PN200-110(PN),diltiazem(Dil)orverapamil(Ver)(100microMeach).Calmodulin(CaM)inhibitedthespecificbindinginadose-dependentmanner(IC50valueofabout100microgprotein/ml).(3)Thespecific125I-omega-CTXMVIIC(60pM)bindingwasinhibitedbyomega-CTXMVIIC,omega-CTXGVIA,omega-CTXSVIB(0.5nMeach),Dyn,Neo&Tob(100microM,each),butnotbyomega-AgaIVA,calciseptine(0.5nMeach),PN,Dil,Ver(100microMeach)or100microgprotein/mlCaM.Theseresultssuggestedthatthecharacteristicsofthespecificbindingof125I-omega-CTXGVIA&125I-omega-CTXMVIICtoCav2.1&Cav2.2channelsintheNBMwereverysimilartothosetocrudemembranesfromchickbrain,althoughtheIC50valuesforCaM&freeCa2+ofCaMwereabout33-&5000-foldhigher,respectively,thanthoseforthespecificbindingof125I-omega-CTXGVIA&125I-omega-CTXMVIICtocrudemembranes.
SeijiIchida, etal. (2005) CharacteristicsofOmega-conotoxinGVIAandMVIICBindingtoCav2.1andCav2.2ChannelsCapturedbyAnti-Ca2+ChannelPeptideAntibodies, NeuRochemicalResearch. PMID: 16076016
N-typecalciumchannelblockers:noveltherapeuticsforthetreatmentofpain
HighlyselectiveCa(v)2.2voltage-gatedcalciumchannel(VGCC)inhibitorshaveemergedasanewclassoftherapeuticsforthetreatmentofchronic&neuropathicpain.ConesnailvenomsprovidedthefirstdruginclasswithFDAapprovalgrantedin2005toPrialt(omega-conotoxinMVIIA,Elan)forthetreatmentofneuropathicpain.Sincethispioneeringwork,majoreffortsunderwaytodevelopalternativesmallmoleculeinhibitorsofCa(v)2.2calciumchannelhavemetwithvariedsuccess.ThisreviewfocusesonthepropertiesoftheCa(v)2.2calciumchannelindifferentpainstates,theactionofomega-conotoxinsGVIA,MVIIA&CVID,describingtheirstructure-activityrelationships&potentialasleadsforthedesignofimprovedCa(v)2.2calciumchanneltherapeutics,&finallythedevelopmentofsmallmoleculesforthetreatmentofchronicpain.
SchroederCl.,  etal. (2006)N-typecalciumchannelblockers:noveltherapeuticsforthetreatmentofpain. MedChem. PMID: 17017994
Smartox生物素ProTx-I电压门控钠通道和T型Cav的阻断剂毒素I（ProTx-1；β-theraphotoxin-Tp1a） 是一种毒素，最初是从Prixopelma pruriens（秘鲁绿色天鹅绒狼蛛）的毒液中分离出来的。此毒素可逆地抑制抗河豚毒素（TTX）的通道 Na v 1.8（IC 50  = 27 nM）和 Na v 1.2，Na v 1.5和Na v 1.7  ，IC 50 值为50至100 nM。此外，  ProTx-I 改变了T型Ca v 3.1通道的电压依赖性活动  （IC 50 = 50 nM），而不会影响灭活的电压依赖性。生物素ProTx-I是ProTx-I的生物素标签版本。