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Fig. 2. From top to bottom, Comparison (mmol/mL) of amino acids in CD patients beforegluten free diet (T) and after diet (s.g.). Six representative amino acids values are reported.Comparison (mmol/mL) of 42 amino acids in CD patients after gluten free diet (S.G.) andhealthy controls (G).study between healthy and celiac subjects let us to hypothesize that amino acids profile inceliac disease can have a diagnostic and/or prognostic value, and that celiac patients candisplay a different amino acids profile compared to healthy ones even if they are followinga gluten free diet. This observation could assume a peculiar importance in the case ofearlier identification of different autoimmune diseases in celiac patients.AcknowledgmentsThis work is supported by Ente Cassa di Risparmio di Firenze and the ANR Chaire d’ExcellencePepKit 2009-2013 (France).References1. Dieterich, W., et al. Nat. Med. 3, 725-726 (1997).2. Stenberg, P., et al. Eur. J. of Medicine 19(2), 83-91 (2008).3. Suresh Babu, S.V., et al. Ind. J. of Clin. Biochem. 17 (2), 7-26 (2002).4. Huub, W.A., Waterval, W.A.H., et al. Clin. Chim Acta 407, 36-42(2009).495
Proceedings of the 31 st European Peptide SymposiumMichal Lebl, Morten Meldal, Knud J. Jensen, Thomas Hoeg-Jensen (Editors)European Peptide Society, 2010Search for Inhibitors or Activators of Human ProteasomeR. Rostankowski 1,2 , E. Jankowska 1 , M. Gaczyńska 3 , P.A. Osmulski 3 ,S. Madabhushi 3 , and F. Kasprzykowski 11 Faculty of Chemistry, University of Gdansk, Sobieskiego 18, 80-952, Gdansk, Poland;2 Department of Biochemistry, University of Texas Southwestern Medical Center, 5323Harry Hines Blvd, Dallas, 75309, TX, U.S.A.; 3 Institute of Biotechnology, University ofTexas Health Science Center, 15355 Lambda Dr, San Antonio, 78245, TX, U.S.A.IntroductionCell metabolism is strictly dependent on number and activity of many different proteins,which are regulated by transcription, translation and post-translative modification, as wellas their irreversible proteolysis effectivity. One of the degradation systems, present ineukaryotic cells, is ATP-dependent ubiquitin-proteasome pathway [1]. Proteasome ismulticatalytic protein complex responsible for intracellular protein degradation. Theproteasome is made up of two subcomplexes: a catalytic core particle (CP; also known asthe 20S proteasome) and one or two terminal 19S regulatory particles (RP) that serves as aproteasome activator with a molecular mass of approximately 700 kDa (called PA700). The19S RP binds to one or both ends of the latent 20S proteasome to form an enzymaticallyactive proteasome 26S. The eukaryotic proteasome is a multicatalytic proteasecharacterized by three activities with distinct specificities against short synthetic peptides: a“chymotryptic-like” activity with preference for tyrosine or phenylalanine at the P1position; a “tryptic-like”activity with preference for arginine or lysine at the P1 position;and a “postglutamyl” hydrolyzing activity with a preference for glutamate or other acidicresidues at the P1 position. [2]. Proteasome activity has a major role in homeostasis of thewhole organism. Disturbance of regular functioning of proteasome is observed in manydiseases, for example neurodegenerative illnesses such as Parkinson, Alzheimer orHuntington [3]. An increase of proteasome activity is also observed in case ofimmunological and pulmonary illnesses like mucoviscidosis [4]. Due to its functionnowadays researchers of the world try to find new regulators of proteasome activity.Results and DiscussionYeast culturing: Saccharomyces cerev, strain MHY501 (kindly provided by MarkHochstrasser, Yale University) was inoculated in YPD medium (yeast extract, peptone,D-Glucose). After culturing, yeast cells wereharvested and processed using microfluidizer andhomogeniztion grinder respectively. Isolated proteinwas purified in three steps: anion exchangechromatography, hydroxyapatite chromatographyand gel filtration as a last step.Purification: Anion exchange chromatographypurification used following protocol: equilibration ofcolumn, direct load, column buffer, 250mM NaCl,400mM NaCl, 1M NaCl with 5-10 min at 4 o C, 500rpm spinning in every stepFig. 1. Proteasome crystals.Hydroxyapatite purification: Purification usedfollowing protocol: 10mM sodium phosphate buffer,100mM, 200mM, 300mM, 400mM and 500mMbuffer with 5 min at 4 o C , 200 g spinning in every step.Gel filtration: Purification proceeded as follows: isocratic separation against gel filtrationbuffer containing: 50 mM Tris-Cl pH 7.0 and 10% glycerol on Superose 6 column. Flowrate 0.4 ml/min and 0.5 ml of fraction volume.Crystallization: Hanging drop vapor diffusion technique was used for the crystallization ofprotesome. The best diffracting crystals (Figure 1) were obtained under followingconditions: 0.03 M Magnessium acetate, 0.1 M MES 7.2, 12% (v/v) MPD. Proteinconcentration used for experiment was 2.5 mg/ml and data were collected using advancesphoton source – beam 19ID (Argonne National Laboratory, Argonne, IL). Structure was496
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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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