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Table 1. The quantity of identified proteins and peptides for each group of samplesExperimental groupsNumber of identifiedproteinsNumber of identifiedpeptidesHealthy donors 290 656Ovarian cancer 178 462Colorectal cancer 137 354Syphilis 158 452Daltonics, Germany). The best generated classification models demonstrated the followingvalues of sensitivity and specificity for the detection of studied diseases: ovarian cancer –100% and 100%; colorectal cancer – 100% and 100%; syphilis – 92% and 100% (forsensitivity and specificity, respectively).Serum samples of all experimental groups were subjected to consecutive separation byWCX and SAX chromatography followed by RP-LC-MS/MS analyses using the Agilent1200 HPLC-Chip/MS Interface coupled with the Agilent 6520 Accurate-Mass Q-TOF. Asa result of MS/MS identification of peptides that was performed by PhenyxServer (GenevaBioinformatics S.A.) using databank Uniprot-SwissProt 1087 unique peptides representing487 proteins were reliably identified (see Table 1) (validation of peptide identifications wasmade by searching MS/MS data against the reversed version of Uniprot-SwissProt).LC-MS/MS analysis of serum samples revealed significant discrepancy betweenidentified peptides and proteins in various experimental groups that contradict visualsimilarity of MALDI-TOF MS profiles between the same groups. Resolution of linearmode of MALDI-TOF mass spectrometers is too low for detail analyses of such complexpeptide mixture as serum is, while a reflector mode is difficult to use because of its lowersensitivity. From the obtained results it is also obvious that it is impossible to correlate thedata of LC-MS/MS identifications with MS peaks of potential biomarkers revealed fromMALDI-TOF MS profiling of serum samples. We believe that high-throughputcomparative MALDI-TOF MS profiling of serum samples can be used for preliminaryestimation of differences between peptide profiles of tested groups, with followingdetection of peptide biomarkers using label-free quantitative LC-MS approach and theirfurther identification by LC-MS/MS.AcknowledgmentsThis work is supported by Russian Foundation for Basic Research (09-04-12085).References1. Anderson, N.L., Anderson, N.G. Mol. Cell. Proteomics 1, 845-867 (2002).2. Mehta, A.I., Ross, S., Lowenthal, M.S., Fusaro, V., Fishman, D.A., Petricoin, E.F., 3 rd , Liotta, L.A.Dis. Markers 19, 1-10 (2003).3. Geho, D.H., Liotta, L.A., Petricoin, E.F., Zhao, W., Araujo, R.P. Curr. Opin. Chem. Biol. 10, 50-55(2006).277
Proceedings of the 31 st European Peptide SymposiumMichal Lebl, Morten Meldal, Knud J. Jensen, Thomas Hoeg-Jensen (Editors)European Peptide Society, 2010The Top-Down Analysis of Chemical Modification of Ubiquitinby ECD MethodPiotr Stefanowicz, Karolina Kowalewska, Monika Kijewska,Alicja Kluczyk, Marek Cebrat, and Zbigniew SzewczukUniversity of Wrocław, Wrocław, 50-137, PolandIntroductionThe ECD (electron-capture dissociation) is a method of choice for top-down analysis ofproteins and large polypeptides. In contrast to CID (collision-induced dissociation)fragmentation method, ECD preserves labile posttranslational modifications. Weinvestigated the nonspecific chemical modification of ubiquitin by ECD method. Theprotein was subjected for glycation [1] and N-phosphorylation [2]. Although thesemodifications are unstable in gas phase during CID experiments, the ECD fragmentation ofglycated and N-phosphorylated peptides provided high sequence coverage. The reactivityof ubiquitin toward glucose [3] and phosphoramidate [2] was investigated. The glycationlevel of lysine moieties as well as N-phosphorylation of histidine residues in ubiquitin wasinvestigated on the intact, chemically modified protein.Results and DiscussionThe high temperature glycation of ubiquitin was performed according to procedurepublished recently by us [3]. The N-phosphorylation of ubiquitin was performed using aA10010+884.98011+808.6311009+988.089RELATIVE ABUNDANCE (%)10+856.97011+844.09911+846.64710+7+7+10+852.569862.614873.175866.75410+889.380RELATIVE ABUNDANCE (%)9+983.1997+3+7+947.8529+973.091996.3858+957.63124+6+ 932.3723+ 1011.0478+922.3391001.8691029.80000840 850 860 870 8800920 940 960 980 1000 1020B600 700 800 900 1000 1100 1200 1300 1400m/z10+1+100390.227RELATIVE ABUNDANCE (%)2+434.2981+1+636.37442+768.487537.3012+693.4042+3+721.077568.8460400 500 600 700865.4999+961.5588+1001081.632RELATIVE ABUNDANCE (%)8+1047.2387+1012.7231+1136.7027+2+1112.2077+1175.6991196.8490 1000 1040 1080 1120 1160400 600 800 1000 1200 1400 1600m/zFig. 1. ECD spectra of chemically modified ubiquitin. A - diglycated protein,B - monophosphorylated protein.278
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Peptides 2010Tales of PeptidesProce
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Peptides 2010Tales of PeptidesProce
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IntroductionWe had the distinct hon
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Scientific programIn planning the 3
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31 st EUROPEAN PEPTIDE SYMPOSIUMSep
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published by John Wiley & Sons as a
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The Josef Rudinger AwardThis award
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Young Investigators' SymposiumThe y
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xxiv
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Design of Peptidyl-Inhibitors for G
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Synthetic Antifreeze Glycopeptide A
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Synthesis and Oxidative Folding of
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Convergent Syntheses of Huprp106-12
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Bactericidal Activity of Small Beta
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Bradykinin Analogues Acylated on Th
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Antimicrobial Activity of Small 3-(
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Interaction of Curcumin with A-Synu
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Fluorescent and Luminescent Fusion
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Cellular Expression of the Human An
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2D IR Spectroscopy of Oligopeptides
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large, non-redundant subset of prot
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The aberrantly glucosylated peptide
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Table 1. Proline cis/trans ratios o
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Table 1. Yields, UV-vis absorption
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Table 1. Purity of the targeted tri
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processes are blocked. Interestingl
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(tb4 n ,1 m )MTII(tb1 n ,4 m )MTIIF
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Fig. 2. a) Part of the 400 MHz HR-M
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Once printed, the amino acid partic
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A) PSA, few seconds73B) PSA, 45 min
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short β strands. In contrast, nume
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neg. control Cs9-Rhd MM-218Fig. 2.
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Table 1. The general structure of t
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% ID in the liver 1 h p.i.100908070
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Peptidyl phosphoranes were first re
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obtained from the same sardines and
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MccJ25 variants were produced by si
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Fig. 2. Proposed signaling mechanis
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Table 1. mCD4-HS12 antiviral activi
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Subject index(S)-2-(1-adamantyl)gly
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chip 18chiral triazine condensing r
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heat stress 348helical conformation
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O-acyl isopeptide method 112obesity
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SH2-ligands 210short collagen-relat
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Author indexAboye, Teshome Leta 142
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Chi, Hongfang 480Chiche, Laurent 6C
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Geronikaki, Athina 444Gessmann, Ren
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Kostova, Kalina 528Kotzia, Georgia
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Nagata, Koji 162Nagayev, Igor Yu. 5
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Salvarese, Nicola 518Sammet, Benedi
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Vauquelin, Georges 138Veiga, Ana Sa
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