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1、ViewOnlineChemCommDynamicArticleLinksCitethis:Chem.Commun.,2011,47,8007–8009www.rsc.org/chemcommCOMMUNICATIONTheeffectofneationicliquidonthefoldingofshortpeptideswJiaLinHuang,zMichaelE.Noss,zKarsonM.Schmidt,LeighMurrayandMichelleR.Bunagan*Received16thMarch2011,Accepted2ndJune2011DOI:10.
2、1039/c1cc11527hUsingcirculardichroismspectroscopy,weshowevidenceofunusualsystemsisdesirableforunderstandingtheeffectofILsonfoldingbehaviourforseveraldesignedpeptidesinneationicliquid.well-definedsecondarystructuresinordertobetterunderstandHelicalpeptides,AKA2andTrp-cage,exhibitheat-induc
3、edfolding,andpredictthecompositeeffectfeltbymorecomplexproteins.withstablehelicalstructurepersistingto968C,whereastheTherefore,inordertoaccomplishthis,wehaveinvestigatedb-hairpinTrpzip4isdestabilizedbytheneat[C4mpy][Tf2N].theeffectof[C4mpy][Tf2N]onmodelpeptides,including8,910designeda-he
4、lixAKA2,mini-proteinTrp-cage,andb-hairpin11Ionicliquids(ILs),organicsaltswhichareliquidsatroomTrpzip4.Theseshortpeptidesareidealtestsystems,aseachtemperature,haverecentlybeenidentifiedasusefulsolventshasbeenwell-studiedandshowntoformstablestructureswithandadditivesforproteinstorage,enzy
5、maticreactions,andwell-characterizedthermalunfolding.1–4ThesequencesofAKA,Trp-cage,andTrpzip4arethegreenchemistry.Withregardstoproteins,theeffectsofILs2assolventsandadditivesvary,assomeprovidethermalresultofpurposefuloptimizationoftheirnativefoldsforstabilization,aggregationsuppression,
6、andenhancedrefold-aqueousconditions.Thealanine-basedhelicalpeptideAKA2abilitywhileothersactasdenaturantsandinduceaggregation.wasdesignedwiththeKAAAArepeatingunittoincludeaOrganicwater-immisciblesolventscanoftenenhanceenzymehighpercentageofAlawithLystoyieldasolublepeptidewith8stabilitya
7、ndreactivityincomparisonwithwater-misciblehighhelicalpropensity.ThestructureofTrp-cageincludesansolventsasthelattermayremoveinternallyboundandN-terminala-helix,ashort310-helix,andaC-terminalpoly-5prolinehelixwhichpacksagainsttheTrp-6toformastrongessentialwatermoleculesfromtheenzyme.I
