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1、ARTICLEpubs.acs.org/BiomacEffectofIonicLiquidsontheSolutionStructureofHumanSerumAlbumin§YasarAkdogan,MatthiasJ.N.Junk,andDariushHinderberger*MaxPlanckInstituteforPolymerResearch,Ackermannweg10,55128Mainz,GermanybSSupportingInformationABSTRACT:Theeffectofseveralionicliquids(ILs)onthesolut
2、ionstructureofhumanserumalbumin(HSA)isrevealedbycontinuouswaveelectronparamagneticresonance(EPR)spectroscopyandnanoscaledistancemeasurementswithdoubleelectron-electronresonance(DEER)spectroscopy.HSA,themostabundantproteininhumanblood,isabletobindandtransportmultiplefattyacids(FAs).Using
3、spin-labeledFA,theuptakeoftheFAbytheproteinandtheirspatialdistributionintheproteincanbemonitored.TheFAdistributionprovidesanindirectyeteffectivewaytocharacterizethestructureoftheproteininsolution.Additionofimidazolium-basedILstoanaqueoussolutionofHSA/FAconjugatesisaccompaniedbysignificant
4、destabiliza-tionandunfoldingoftheprotein’stertiarystructure.Incontrast,HSAmaintainsitstertiarystructurewhencholinedihydrogenphosphate(dhp)isadded.ThecomparisonofFAdistancedistributionsinHSAwithandwithoutcholinedhpsurprisinglyrevealedthatwiththisIL,theFAanchoringunitsareinbetteragreement
5、withthecrystallographicdata.Furthermore,theFAentrypointdistributionappearswidenedandmoreasymmetricthaninpurebuffer.TheseresultsindicatethatcholinedhpasacosolventmayselectivelystabilizeHSAconformationsclosertothecrystalstructureoutoftheoverallconformationalensemble.’INTRODUCTIONdifferentia
6、lscanningcalorimetry,fluorescencespectroscopy,Fouriertransforminfraredspectroscopy,UV-visspectroscopy,Ionicliquids(ILs)haveattractedextensiveattentionduring4-6,10,12-17andsmall-angleneutronscattering.InthisArticle,recentyearsbecauseoftheirpotentialinvariousbiologicalandweintroduceelectro
7、nparamagneticresonance(EPR)spec-pharmaceuticalapplications.Specifically,theirabilitytosolubilizeandtroscopyasanalternativetechniquetocharacterizetheeffectsstabilizeproteinsinvitroforextendedtimeswasextensively1-6ofILsonthefunctionalstructureofhumanserumalbuminstudied.Theuniquefea
