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Smartox/Blocker of Nav1.1 / 1.2 / 1.3 / 1.4 / 1.6 / 1.7/12GSF002-00500/0.5mg
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GsAF-II (alsotermedKappa-theraphotoxin-Gr2c,GsAF-2)wasoriginallyisolatedfromthevenomofGrammostolaroseaspider. GsAF-II peptidetoxinhasantinociceptiveandantiarrhythmiceffectsinmammals.Thepeptideisreportedtoblockthefollowingvoltage-gatedsodiumchannels:Nav1.1,Nav1.2,Nav1.3,Nav1.4,Nav1.6andNav1.7withIC50 valuesof,respectively,5.7,12,24,4,6.6and1.3µM.ThispeptidealsoblockshERG1withanIC50 valueof4.7µM.Description:Productcode:N/A.Category:Sodiumchannels.Tags:nav,tetrodotoxin,ttx.AAsequence: Tyr-Cys2-Gln-Lys-Trp-Met-Trp-Thr-Cys9-Asp-Glu-Glu-Arg-Lys-Cys15-Cys16-Glu-Gly-Leu-Val-Cys21-Arg-Leu-Trp-Cys25-Lys-Lys-Lys-Ile-Glu-Trp-OHDisulfidebonds: Cys2-Cys16,Cys9-Cys21,andCys15-Cys25)Length(aa): 31Formula: C176H261N47O45S7MolecularWeight: 3979.78DaAppearance: WhitelyophilizedsolidSolubility: aqueousbufferCASnumber: notavailableSource: SyntheticPurityrate: >98%Reference:TargetPromiscuityandHeterogeneousEffectsofTarantulaVenomPeptidesAffectingNa+andK+IonChannelsVenom-derivedpeptidemodulatorsof ion channelgatingareregardedasessentialtoolsforunderstandingthemolecularmotionsthatoccurduringtheopeningandclosingof ion channels.Inthisstudy,wepresentthecharacterizationoffivespidertoxinson12humanvoltage-gated ion channels,followingobservationsaboutthe target promiscuity ofsomespidertoxinsandtheongoingrevisionoftheir“canonical”gating-modifyingmodeofaction.The peptides werepurifieddenovofromthe venom ofGrammostolaroseatarantulas,andtheirsequenceswereconfirmedbyEdmandegradationandmassspectrometryanalysis.Their effects onseventetrodotoxin-sensitive Na(+) channels,thethreehumanether-à-go-go(hERG)-related K(+) channels,andtwohumanShaker-related K(+) channels wereextensivelycharacterizedbyelectrophysiologicaltechniques.Allthepeptides inhibited ion conductionthroughallthe Na(+) channels tested,althoughwithdistinctivepatterns.The peptides alsoaffectedthethreepharmaceuticallyrelevanthERGisoformsdifferently.Athigherconcentrations,all peptides alsomodifiedthegatingofthe Na(+) channels byshiftingtheactivationtomorepositivepotentials,whereasmorecomplex effects wererecordedonhERG channels.No effects wereevidentonthetwoShaker-related K(+) channels atconcentrationswellabovetheIC(50)valuefortheaffected channels.Giventhesequencediversityofthetestedpeptides,weproposethat tarantula toxinsshouldbeconsideredbothasmultimodeand target-promiscuous ion channelmodulators;bothfeaturesshouldnotbeignoredwhenextractingmechaNISTicinterpretationsabout ion channelgating.Ourobservationscouldalsoaidinfuturestructure-functionstudiesandmighthelpthedevelopmentofnovel ion channel-specificdrugs.ELISARedaelli,etal.(2010)TargetPromiscuityandHeterogeneousEffectsofTarantulaVenomPeptidesAffectingNa+ andK+ IonChannels. JBC. PMID: 19955179
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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