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Smartox//MAM001-50010/5x.0.01mg
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ASIC1a&1bchannelblockerMambalgin-1wasinitiallyisolatedbySylvieDiochotandcollaboratorsfromthevenomoftheblackmamba(Dendroaspispolylepispolylepis).Mambalgin-1isapotentandselectiveblockerofacid-sensingionchannels(ASIC).ASICchannelshavebeendemonstratedtobeimpliedinpainpathwaysandappeartobepromisingtherapeutictargets. Mambalgin-1rapidlyandreversIBLyinhibitsrecombinanthomomericASIC1a(IC50=55nM)andheteromericASIC1a+ASIC2a(IC50=246nM)orASIC1a+ASIC2bchannels(IC50=61nM)butalsohumanchannelshASIC1b(IC50=192nM)and hASIC1a+hASIC1b(IC50=72nM).Mambalgin-1belongstothefamilyofthree-fingertoxinsandhasnosequence/structuralhomologywitheitherPcTx1orAPETx2.Mambalgin-1differsfrommambalgin-2byoneaminoacid.Bothhavedemonstratedasimilaractivity.Mambalgin-1hasnoeffectonASIC2a,ASIC3,ASIC1a+ASIC3andASIC1b+ASIC3channels,aswellasonTRPV1,P2X2,5-HT3A,Nav1.8,Cav3.2andKv1.2channels.RecentlyquotedFig1: Dose-responsecurveoftheeffectofsyntheticMambalgin-1#MAM001onASIC1acurrentrecordedin Xenopusoocytes.Inthissystem,anIC50of21nMwasdetermined.Description:Productcode:MAM001.Category:ASICchannels.Tags:acidsensing,apetx2,ASIC,pain,PcTx1,psalmotoxin.AAsequence:LKC3YQHGKVVTC12HRDMKFC19YHNTGMPFRNLKLILQGC37SSSC41SETENNKC49C50STDRC55NK-OHDisulfidebonds:Cys3-Cys19,Cys12-Cys37,Cys41-Cys49,Cys50-Cys55Length(aa):57Formula: C272H429N85O84S10MolecularWeight: 6554.59DaAppearance:whitelyophilizedsolidSolubility: waterorsalinebufferCASnumber:notavailableSource:syntheticPurityrate: >98%Reference:Blackmambavenompeptidestargetacid-sensingionchannelstoabolishpain.DiochotS.,etal.(2012)Blackmambavenompeptidestargetacid-sensingionchannelstoabolishpain.Nature.PMID:23034652Polypeptidetoxinshaveplayedacentralpartinunderstandingphysiologicalandphysiopathologicalfunctionsofionchannels.Inthefieldofpain,theyledtoimportantadvancesinbasicresearchandeventoclinicalapplications.Acid-sensingionchannels(ASICs)aregenerallyconsideredprincipalplayersinthepainpathway,includinginhumans.AsnaketoxinactivatingperipheralASICsinnociceptiveneuronshasbeenrecentlyshowntoevokepain.Hereweshowthatanewclassofthree-fingerpeptidesfromanothersnake,theblackmamba,isabletoabolishpainthroughinhibitionofASICsexpressedeitherincentralorperipheralneurons.Thesepeptides,whichwecallmambalgins,arenottoxicinmicebutshowapotentanalgesiceffectuponcentralandperipheralinjectionthatcanbeasstrongasmorphine.Thiseffectis,however,resistanttonaloxone,andmambalginscausemuchlesstolerancethanmorphineandnorespiratorydistress.PharmacologicalinhibitionbymambalginscombinedwiththeuseofknockdownandknockoutanimalsindicatesthatblockadeofheteromericchannelsmadeofASIC1aandASIC2asubunitsincentralneuronsandofASIC1b-containingchannelsinnociceptorsisinvolvedintheanalgesiceffectofmambalgins.Thesefindingsidentifynewpotentialtherapeutictargetsforpainandintroducenaturalpeptidesthatblockthemtoproduceapotentanalgesia.CharacterizationofhASIC1achannelsupontoxinmambalgin-1bindinginlivemammaliancellsWenM.,etal. (2015)Site-specificfluorescencespectrumdetectionandcharacterizationofhASIC1achannelsupontoxinmambalgin-1bindinginlivemammaliancells.ChemCommun.PMID: 25873388Thesynthesisoffluorescentunnaturalamino-acidAnapwasoptimizedandtheAnapwasincorporatedintofoursitesinanacid-pocketoratransmembraneregionofhumanacid-sensingionchannel-1a(hASIC1a).CombinationalAnapfluorescencespectraandpatch-clampelectrophysiologydataillustratedsite-specificconformationalresponsesupontoxinmambalgin-1binding.Thiscombinationalapproachcanbeusedtoanalyseconformationalpropertiesofmanydifferenteukaryoticproteinsintheirfunctionalstates,inasite-specificmannerinlivemammaliancells.Bindingsiteandinhibitorymechanismofthemambalgin-2SalinasM.,etal.(2014)Bindingsiteandinhibitorymechanismofthemambalgin-2pain-relievingpeptideonacid-sensingionchannel1a.JBC.PMID:24695733Acid-sensingionchannels(ASICs)areneuronalproton-gatedcationchannelsassociatedwithnociception,fear,depression,seizure,andneuronaldegeneration,suggestingrolesinpainandneurologicalandpsychiatricdisorders.Wehaverecentlydiscoveredblackmambavenompeptidescalledmambalgin-1andmambalgin-2,whicharenewthree-fingertoxinsthatspecificallyinhibitwiththesamepharmacologicalprofileASICchannelstoexertstronganalgesiceffectsinvivo.Wenowcombinedbioinformaticsandfunctionalapproachestouncoverthemolecularmechanismofchannelinhibitionbythemambalgin-2pain-relievingpeptide.Mambalgin-2bindsmainlyinaregionofASIC1ainvolvingtheupperpartofthethumbdomain(residuesAsp-349andPhe-350),thepalmdomainofanadjacentsubunit,andtheβ-balldomain(residuesArg-190,Asp-258,andGln-259).Thisregionoverlapswiththeacidicpocket(pHsensor)ofthechannel.ThepeptideexertsbothstimulatoryandinhibitoryeffectsonASIC1a,andweproposeamodelwheremambalgin-2trapsthechannelinaclosedconformationbyprecludingtheconformationalchangeofthepalmandβ-balldomainsthatfollowsprotonactivation.ThesedatahelptounderstandinhibitionbymambalginsandprovidecluesforthedevelopmentofnewoptimizedblockersofASICchannels.
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) ”。
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