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1、Anal.Chem.2010,82,10471053PhosphopeptideScreeningUsingNanocrystallineTitaniumDioxideFilmsasAffinityMatrix-AssistedLaserDesorptionIonizationTargetsinMassSpectrometry††††,‡§Marie-LuiseNiklew,UlrikeHochkirch,AnnaMelikyan,ThomasMoritz,SandraKurzawski,§†,†HartmutSchlu¨ter,IngoEbner,andMichaelW.L
2、inscheid*DepartmentofChemistry,Humboldt-UniversitaetzuBerlin,Berlin,Germany,AnalyticalLaboratories,AtotechGmbH,Berlin,Germany,andDepartmentofClinicalChemistry/CentralLaboratories,UniversityMedicalCenter,Hamburg-Eppendorf,GermanyTheuseofnanocrystallinetitaniumdioxidefilmsasactincancermakesth
3、eirresults,thephosphorylatedproteins,3affinitytargetsfortheselectiveisolationandenrichmentevenmoreinteresting.Therefore,thedetectionofphosphorylatedofphosphopeptideswithsubsequentanalysisbymatrix-proteinsisamajorchallenge.assistedlaserdesorptionionization(MALDI)massspec-Theenzymaticdigestio
4、nofaproteinextractgenerallyrequiredtrometryisdescribed.Astrongaffinityofphosphopep-foritsanalysisresultsmostlyinthegenerationofnumeroustidestoanatasetitaniumdioxidesurfacesisobserved,andpeptides.Theoverwhelmingnumberofpeptidesincombinationastandardprotocolfortheselectiveisolationandenrich-w
5、ithsubstoichiometricamountsofphosphorylatedpeptidesmentofphosphopeptidesontitaniumdioxidefilmsusingdecreasesthechanceoftheirdetectionsignificantly.Besidetheaproteolyticdigestofr-and-caseinwasdeveloped.Allfactofphosphorylation,thenatureofthemodifiedaminoacidwashingandelutionproceduresusingthe
6、sefilmscanbewithinthesequenceisofinterest,andtheassignmentoftheprocesseddirectlyontheMALDItarget,therebyavoidingphosphorylationsiteisamajorchallengeinproteinanalysis.samplecontaminationandlosses.Inaddition,theenrich-Asmostproteomicsapproachesusemassspectrometryasthementofthephosphopeptidesw
7、asimprovedduetoaanalyticaltool,itoffersseveralpossibilitiesinthedetectionofpost-considerableenlargementofthesurface.Severalfilm4,5translationalmodifications,too.Afterasuccessfulseparationsubstratescompatiblewithroutineinletsystemsofmassofthepeptides,tandemmasssp
