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Identity of the protein was checked by mass spectrometry, while the proper refolding waschecked by Circular Dichroism measurements.The antibody absorbance (Figure 1) to the expressed rMOG ED (His) 6 was evaluated byindirect ELISA using patients [Multiple Sclerosis sera (MS) and cerebrospinal fluid(MS-CSF)] and controls [other neurological diseases (OND), rheumatoid arthritis (RA),and blood donors (BD)].Fig. 1. Column scatter of the ELISA absorbance values to the rMOG ED (His) 6 in MS,MS-CSF, OND, RA, BD.Antibodies were detected in a few sera and in no CSF. No difference existed between boththe groups for IgM while for IgG there were borderline differences among sera groups(Kruskal-Wallis Test, p
<strong>Proceedings</strong> of the 31 st European Peptide SymposiumMichal Lebl, Morten Meldal, Knud J. Jensen, Thomas Hoeg-Jensen (Editors)European Peptide Society, 2010The Metabolisation of Different Iodinated Peptide SpeciesBart De Spiegeleer 1 , Sylvia Van Dorpe 1 , and Ewald Pauwels 21 Drug Quality and Registration (DruQuaR) group, Faculty of Pharmaceutical Sciences,Ghent University, Ghent, 9000, Belgium; 2 Department of Subatomic and RadiationPhysics, Faculty of Sciences, Ghent University, Ghent, 9000, BelgiumIntroductionRadio-iodinated peptides are frequently used in biomedical research (e.g. blood-brainbarrier transport studies) and diagnostic-therapeutic clinical applications. Up till now, onlytwo enzyme systems are known to be responsible for dehalogenation: iodotyrosinedeiodinase (IYD) and iodothyronine deiodinase (ID) [1-3]. However, currently, onlyiodinated amino acids and thyroid hormones have been investigated [4], but no systematicstudy on the metabolisation of iodinated peptides has been published. It is reported thatenzymatic degradation and deiodination occurs in vitro as well as in vivo [5,6]. Therefore,the in vitro stability of different iodinated mouse obestatin peptides was characterised in themain metabolic <strong>com</strong>partments: plasma, liver and kidney. The degradation kinetics andmetabolites of the iodinated obestatin peptides arising from both enzymatic proteolysis anddehalogenation is evaluated.Results and DiscussionThe in vitro first order degradation kinetics results obtained on the different iodinatedobestatin peptides in different biological matrices using HPLC with UV detection at 195nm are summarized in Table 1. Although iodine incorporation is considered to potentiallyhinder peptide breakdown byprotease activity, a statisticallysignificant (i.e. based upon the95% confidence intervals)increase in half life time wasonly observed for (DIP (Tyr))-obestatin in plasma and for(MIP (Tyr))-obestatin in liverhomogenate. Several obestatinmetabolites arising fromproteolytic activity wereobserved using (tandem) massspectrometry (Figure 1).Both in plasma and liverhomogenate, the peptide bondbetween Phe 5 and Asp 6 wasfound to be more susceptibleto proteolytic cleavage for theiodinated peptide withFig. 1. A graphical overview of the proteolytic cleavagesobserved at T 20min in plasma (left) and liver (right).Significant proteolysis is indicated by , followed by lessimportant cleavage and least important .reference to the native peptide.In plasma, the abundance ofcleavages near the C-terminusof the sequence (i.e. Leu 11 toLeu 23 ) was found to decreaseupon peptide iodination, e.g.Arg 21 -Ala 22 . In liver, a similar effect was observed for the cleavage at Gly 20 -Arg 21 , togetherwith an inhibition of the Tyr 16 -Gln 17 peptide bond proteolysis for the two Tyr 16 -iodinatedobestatin derivatives.502
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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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Proceedings of the 31 st European P
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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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