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Fig. 3. GC-MS n analysis of culture media (a) without treatment, (b) AgNPs treated.To specifically monitor effects of AgNPs on cell wall PGN glycan strands, the amount ofMuramic acid (MA), released into the culture media was studied. For this purpose, GC-MS n was carried out before and after treatment. It can be seen from Figure 3b that AgNPstreatment caused an increase in MA concentration in the culture medium.Studies demonstrated that PGNs should be digested for HPLC analysis.We hypothesized that, as PGNs structure were broken by AgNPs treatment, theproduced fragments can be monitored using HPLC/MS n analyses. Increase of the lowmolecular weight fractions on the HPLC chromatogram after AgNPs treatment willapprove our hypothesis, that they caused PGN breakage. The MS n analysis of them hasbeen performed usingmass spectrometry. Itcan be seen from thePGN standard solutionsample (Figure 4a) thefragments higher than2500 m/z. On the otherhand the treatment ofAgNPs caused somebreakage of PGNsstructure, which isshown on part Figure4b. From that treatmentmore fragmentation onPGN with low molecularweight, (fragmentslower than 2800m/z) were obtained.These results indicatethat the reaction withAgNPs affects thepeptide primary structureand increasing thenumber of degradationproducts after thesePGNs treatment.Fig. 4. Mass Spectrometry analysis of the PGN standardsolution sample (a), and after the AgNPs treatment (b) ofPGNs, using Finigan LCQ deca ion trap instrumentation.References1. Shrivastava, S., et al.Nanotechnology 18, 225103 (2007).2. Dibrov, P., et al. Antimicrob. Agents Chemother. 46, 2668-2670 (2002).3. Vollmer, W., Blanot, D., de Pedro, M.A. FEMS. Microbiol. Rev. 32, 149-167 (2008).275
Proceedings of the 31 st European Peptide SymposiumMichal Lebl, Morten Meldal, Knud J. Jensen, Thomas Hoeg-Jensen (Editors)European Peptide Society, 2010Peptidomic Analysis of Human Blood Serum for SpecificDisease MarkersRustam H. Ziganshin, Georgii P. Arapidi, Igor V. Azarkin,Vadim M. Govorun, and Vadim T. IvanovDepartment of Proteomics, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry,Russian Academy of Sciences, Moscow, 117997, RussiaIntroductionBlood and its derivatives (plasma and serum) is very attractive for a biomarker studies dueto the unique properties of this liquid connective tissue, which comes into contact withpractically all cells in the organism absorbing some traces of their metabolic activity,including markers of disease-induced metabolic change [1]. Albumin, immunoglobulins,and other proteins that are present in blood in very high concentrations are known to bindto and transport various low-molecular compounds, including small proteins and peptides[2]. As a result, these compounds are protected from removal from the bloodstream bykidneys and can be accumulated in blood in considerable amounts. It has been suggestedthat this peptidome may serve as an important source of clinical diagnostic information [3].Results and DiscussionA simple and reproducible method of peptide desorption from abundant blood proteins wasdeveloped. This method increases the quantity of peptides detected in serum samples byMALDI-TOF MS and improves the quality and reproducibility of the recorded MSprofiles. Blood serum samples obtained from 39 patients with ovarian cancer, 42 patientswith colorectal cancer, 72 patients with syphilis and 200 healthy donors were fractionatedusing a profiling kit containing MB-WCX surface-functionalized magnetic beads (BrukerDaltonics, Germany) according to the manufacturer’s protocols, with small modifications.MALDI-TOF MS data of fractionated serum samples (Figure 1) were acquiredautomatically in a linear mode using ultraflex TM mass spectrometer (Bruker Daltonics,Germany). MS data analyses, classification models generation and validation were madeusing software for biomarker detection and evaluation – ClinProTools 2.1 (BrukerFig. 1. MALDI-TOF MS profiles of the same serum sample fractionated on MB-WCXmagnetic beads before (A) and after (B) heating. The spectrum intensity and m/z values(Da) are plotted along the Y-axis and X-axis, respectively.276
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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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