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Table 1. Proteins identified by MALDI-TOF and further confirmed by MS/MS analysisSDS-WB band(kDa)Protein identifiedIDscore(thld)47kDa [1] 2’,3’-Cyclic-Nucleotide 3- I56577 94(63) 4.4e-05Phosphodiesterase (Rat)47kDa [2] Creatine kinase (Rat) Q499P7_rat 90(63) 1.2e-0498kDa Brain specific alpha actinin (Rat) Q6T487_rat 83(63) 5.7e-04130kDa Spectrin alpha chain or Alpha fodrin (Rat) AAC33127 133(63) 6.1e-09sig.(a) (b)RU756555453525155-5Monoclonal IgGs binding analysis on CSF114(Glc) coated chip in SPRAlpha actinin (Sigma) Alpha fodrin (Abcam) CNPase (Abcam) Creatine kinase BB(Abcam)Monoclonal IgGs 10ug/mlFig. 2. (a) Western blot of rat brain proteins with affinity purified anti-CSF114(Glc) IgGsfrom Multiple Sclerosis patients’ sera (lane A, B, C) and anti-CSF114(Glc) IgGs from onerepresentative normal blood donor (lane D). (b) Surface Plasmon Resonance of identifiedcytoskeletal proteins monoclonal IgGs (Sigma, Abcam) on CSF114(Glc)-coated chip.Further confirmation was obtained using commercially available monoclonal antibodies toAlpha fodrin, Creatine kinase BB, and CNPase (Abcam), and Alpha actinin (Sigma). All themonoclonal IgGs were used in Surface Plasmon Resonance (BIAcore T100 TM ) for bindinganalysis with CSF114(Glc)-coated chips. Interestingly, we found that anti-Alpha fodrin,anti-Creatine kinase BB, and anti-Alpha actinin monoclonal IgGs were able to bind withCSF114(Glc). Differently anti-CNPase IgGs did not display any binding at the sameconcentration (Figure 2).In conclusion, we characterized for the first time that the artificially designedCSF114(Glc) specifically recognizes anti-Alpha fodrin and anti-Alpha actinin monoclonalIgGs, belonging to the same family of cytoskeletal proteins.The question arising now: are the proteins Alpha fodrin, Creatine kinase BB, andAlpha actinin real native antigens involved in triggering autoantibody-mediated MultipleSclerosis?AcknowledgmentsItalian government scholarship for biotechnology 2008 (India) and MIUR scholarship 2009 (Italy) toS.P., Ente Cassa Risparmio di Firenze (Italy) as well as Chaire d’Excellence 2009-2013 (France) toA.M.P. are gratefully acknowledged for financial support.References1. Papini, A.M., et al. Granted U.S.A. Patent & PCT WO 03/000733 A2.2. Papini, A.M. Simple test for multiple sclerosis. Nat. Med. 11, 13 (2005).3. Carotenuto, A., et al. J. Med. Chem. 51, 5304-5309 (2008).4. Lolli, F., et al. P.N.A.S. 102, 10273 (2005).5. Lolli, F., et al. J. Neuroimmunol. 167, 131 (2005).291
Proceedings of the 31 st European Peptide SymposiumMichal Lebl, Morten Meldal, Knud J. Jensen, Thomas Hoeg-Jensen (Editors)European Peptide Society, 2010Role of Triple Hyp→Pro Substitution on Conformation andBioactivity of Integramide AMarta De Zotti 1 , Wim De Borggraeve 2 , Bernard Kaptein 3 ,Quirinus B. Broxterman 3 , Sheo B. Singh 4 , Peter J. Felock 5 ,Daria J. Hazuda 5 , Fernando Formaggio 1 , and Claudio Toniolo 11 ICB, Padova Unit, CNR, Department of Chemistry, University of Padova, Padova, 35131,Italy; 2 Department of Chemistry, Catholic University Leuven, Leuven, 3001, Belgium;3 DSM Innovative Synthesis BV, Geleen, 6160 MD, The Netherlands; 4 Medicinal Chemistry,Merck Research Laboratories, West Point, 19486, PA, U.S.A.; 5 Medicinal Chemistry,Merck Research Laboratories, Rahway, 07065, NJ, U.S.A.IntroductionAIDS is produced by HIV-induced infections. HIV integrase is an important enzyme as it iscritical for the integration of HIV genome into that of the host cell. Because this complexprocess is exclusively brought about by the virus, the enzyme, not found in the host cell,represents a safe target for the development of a single or a combined anti-HIV therapy.Integramide A is a 16-mer long, effective peptaib inhibitor of HIV-1 integrase. Its primarystructure is: Ac-D-Iva-L-Hyp-L-Iva-L-Leu-Aib-Aib-Aib-L-Hyp-L-Iva-D-Iva-Gly-OH (Ac,acetyl; Aib, α-aminoisobutyric acid; Hyp, (4R)-hydroxyproline; Iva, isovaline) [1].Results and DiscussionWe have recently described a versatile synthetic strategy in solution to afford this naturalcompound and its diastereomer at positions 14 and 15, and found that both peptides displaya significant inhibitory activity [2]. In this study, we present our data on the synthesis insolution, in-depth FT-IR absorption, CD and 2D-NMR conformational analysis (Figure 1),and biological activity against HIV-integrase (Table 1) of the analogues of the two abovementioned peptides in which all of the three (2S,4R)-Hyp residues at positions 2, 9, and 13are replaced by L-Pro.IIIFig. 1. (I) Superposition of the 22 lowest-energy backbone, mixed α-/3 10 - helical 3Dstructures(energy < 129 Kcal/mol) for the integramide A analogue containing the -L-Iva 14 -D-Iva 15 - sequence consistent with the 2D-NMR derived distances and dihedral anglerestraints. (II) Ribbon representation of the lowest-energy 3D-structure obtained for thesame peptide. The three L-Pro residues are labeled.292
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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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