Journal of Peptide Science

Cover image for Vol. 19 Issue 2

February 2013

Volume 19, Issue 2

Pages 65–126

  1. Research Articles

    1. Top of page
    2. Research Articles
    1. Investigation of peptide thioester formation via N[RIGHTWARDS ARROW]Se acyl transfer (pages 65–73)

      Anna L. Adams and Derek Macmillan

      Version of Record online: 7 JAN 2013 | DOI: 10.1002/psc.2469

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      A fast, new route to peptide thioesters is presented, using selenocysteine at the C-terminus of peptides prepared from solid-phase peptide synthesis. Thioester formation is initiated via an N[RIGHTWARDS ARROW]Se acyl shift and can occur at lower temperatures and in shorter time scales than previously seen when using cysteine in this way. This strategy also has been shown to accelerate the cyclization of an antimicrobial peptide.

    2. Critique of the use of fluorescence-based reporters in Escherichia coli as a screening tool for the identification of peptide inhibitors of Aβ42 aggregation (pages 74–83)

      Oliver Wright, Liao Zhang, Yun Liu, Tatsuya Yoshimi, Yizhi Zheng and Alan Tunnacliffe

      Version of Record online: 16 DEC 2012 | DOI: 10.1002/psc.2474

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      In vivo screening of a quasi-random peptide library in E. coli expressing Aβ-GFP was used to identify peptides with anti-aggregation activity. Although we successfully defined novel peptide activities, unforeseen problems can arise with such biosynthetic in vivo strategies due to the inherent noise in biological systems and we critique the approach in this light.

    3. The mapping of linear B-cell epitope regions in the extracellular parts of the desmoglein 1 and 3 proteins: recognition of immobilized peptides by pemphigus patients' serum autoantibodies (pages 84–94)

      Hajnalka Szabados, Szilvia Bősze, Pálma Silló, Sarolta Kárpáti, Ferenc Hudecz and Katalin Uray

      Version of Record online: 8 JAN 2013 | DOI: 10.1002/psc.2476

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      Pemphigus specific epitope regions were identified in desmoglein 1 and 3 proteins with pin-bound synthetic 15-mer peptides and modified ELISAs by testing serum antibodies from patients and healthy donors. The serum antibodies of the healthy individuals did not show any specific recognition. Not only conformational but also linear epitope regions are spread in the entire extracellular region of the desmoglein 1 protein.

    4. Identification and mapping of a linear epitope of centromere protein F using monoclonal antibodies (pages 95–101)

      Simon Welner, Nicole H. Trier, Gunnar Houen and Paul R. Hansen

      Version of Record online: 7 JAN 2013 | DOI: 10.1002/psc.2478

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      Autoantibodies against centromere protein F have been reported to be associated with various types of cancer with poor prognosis. In this study, we mapped the epitope (NELSRIRSEKA) recognized by two monoclonal centromere protein F using synthetic peptides.

    5. Production and initial structural characterization of the TM4TM5 helix-loop-helix domain of the translocator protein (pages 102–109)

      C. Galvagnion, P. Montaville, Y.-M. Coïc and N. Jamin

      Version of Record online: 13 JAN 2013 | DOI: 10.1002/psc.2468

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      The translocator protein is a small essential membrane protein, involved in the translocation of cholesterol across mitochondrial membranes. Here, we present the study of its double transmembrane domain encompassing the last two C-terminal helices (TM4TM5). The protocol of production of TM4TM5 with more than 95% purity is reported. Far-UV circular dichroism studies indicate that the secondary structure of TM4TM5 in various detergent micelles is highly helical and preliminary NMR analysis indicates that TM4TM5 adopts a stable tertiary fold within the TM4TM5-DHPC complex.

    6. Introduction of histidine units using benzotriazolide activation (pages 110–117)

      Kiran Bajaj, Siva S. Panda, Mohamed A. Ibrahim, Said A. El-Feky and Alan R. Katritzky

      Version of Record online: 16 JAN 2013 | DOI: 10.1002/psc.2483

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      Histidine-containing peptides and histidine conjugates were prepared using Nα-Boc-Nim-(4-toluenesulfonyl-l-histidylbenzotriazole) as active intermediate.

    7. Interactions of vasopressin and oxytocin receptors with vasopressin analogues substituted in position 2 with 3,3′-diphenylalanine – a molecular docking study (pages 118–126)

      Magdalena J. Ślusarz, Emilia Sikorska and Rafał Ślusarz

      Version of Record online: 10 JAN 2013 | DOI: 10.1002/psc.2485

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      Four vasopressin analogues substituted at position 2 with 3,3′-diphenylalanine have been docked into partially flexible vasopressin/oxytocin receptors. The bulky residue at position 2 acts as a structural restraint much stronger in the oxytocin receptor than in the vasopressin V2 receptor. A weak activity at V1a vasopressin receptor appears to be caused by weak receptor–ligand interactions. Results of this study may facilitate a rational design of new analogues with the highest activity/selectivity at vasopressin and oxytocin receptors.

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