Biochemical engineering of the N‐acyl side chain of sialic acids alters the kinetics of a glycosylated potassium channel Kv3.1

摘要

ThesialicacidofcomplexN‐glycanscanbebiochemicallyengineeredbysubstitutingthephysiologicalprecursorN‐acetylmannosaminewithnon‐naturalN‐acylmannosamines.TheKv3.1glycoprotein,aneuronalvoltage‐gatedpotassiumchannel,containssialicacid.WesternblotsoftheKv3.1glycoproteinisolatedfromtransfectedB35neuroblastomacellsincubatedwithN‐acylmannosaminesverifiedsialylatedN‐glycansattachedtotheKv3.1glycoprotein.OutwardioniccurrentsofKv3.1transfectedB35cellstreatedwithN‐pentanoylmannosamineorN‐propanoylmannosaminehadsloweractivationandinactivationratesthanthoseofuntreatedcells.Therefore,theN‐acylsidechainofsialicacidisintimatelyconnectedwiththeactivationandinactivationratesofthisglycosylatedpotassiumchannel...