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1、ReviewTHEINTERPRETATIONOFCOLLISION-INDUCEDDISSOCIATIONTANDEMMASSSPECTRAOFPEPTIDESloannisA.PapayannopoulosBiogenZnc.,14CambridgeCenter,Cambridge,Massachusetts02142I.INTRODUCTIONTheintroductionoffastatombombardment(FABJionizationmassspec-trometry(MSJ(1)intheearly1980senabledmass
2、spectrometriststoobtainmolecularweightsofmanynonvolatilemolecules,includingpeptidescomprising10-20aminoacids,and,bythemid-1980s.smallproteinscouldbedesorbedandtheirmolecularweightsmeasured(2-7).FAB(hereusedgenericallytoincludefastatomaswellasionbombard-mentofthesampledissolved
3、inaliquidmatrixsuchasglycerol),beinga”softionization”technique,produceslittleornofragmentationofproton-atedpeptidemolecules.Thischaracteristicis,certainly,desirable,becauseitallowsfortheunambiguousassignmentofmolecularweights,eveninmulticomponentmixtures.Nevertheless,fragmenta
4、tionofamolecule,afterionizationinthemassspectrometer,canbeusedtoobtainstructuralinformation,oftencompletelyanduniquely,andfordecadesmassspectraofthousandsofcompoundshavebeenacquired,interpreted,andcataloged.Peptidesconsistingofasfewasseveralaminoacidsarenonvolatileand,often,th
5、ermallylabileandcannotbeintroducedintothemassspectrometerinthegasphasewithoutpriorderivatization.Derivat-izedpeptideshavebeensuccessfullyfragmented,primarilyusingelectronimpact(El)ionization,andtheiraminoacidsequencedetermined(8-13).sometimeswiththeassistanceofcomputerprograms
6、(14).Complexmixturesofproteinenzymedigests,oftenfollowedbypartialacidhy-drolysis,werederivatizedandintroducedintothemassspectrometerafterfractionationwithagaschromatograph(GC).TheElspectrawereusedtoobtainaminoacidsequencesforthepeptides,whichweresubsequentlycombinedtoarriveatt
7、hesequenceoftheprotein.Peptidefragments,whichsometimesareproducedduringFABioniza-tion,canbecorrelatedtothepeptideaminoacidsequence(15-20).Theabundanceofsuchfragmentions,however,isquitelowcomparedwiththeionsduetotheprotonatedmolecule.Inaddition,inordertoobtainreasonablyabundant
8、fragmentions,afairlyconcentratedsampleisrequired,andeventhenl
