Journal of Peptide Science

Cover image for Vol. 20 Issue 8

August 2014

Volume 20, Issue 8

Pages i–iii, 595–667

  1. Issue Information

    1. Top of page
    2. Issue Information
    3. Review
    4. Research Articles
    1. Issue information (pages i–iii)

      Version of Record online: 13 JUL 2014 | DOI: 10.1002/psc.2563

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  2. Review

    1. Top of page
    2. Issue Information
    3. Review
    4. Research Articles
    1. Biogenesis of d-amino acid containing peptides/proteins: where, when and how? (pages 595–612)

      Céline Ollivaux, Daniel Soyez and Jean-Yves Toullec

      Version of Record online: 3 JUN 2014 | DOI: 10.1002/psc.2637

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      It is well known that proteins can display in its chain an amino acid in the d-configuration Several hypotheses may be formulated to explain the origin of a d-residue in the peptide chain. The different pathways of biogenesis of d-amino acid containing peptides in bacteria and multicellular organisms are reviewed, along with the description of the cellular specificity, the enzyme specificity and the substrate specificity of peptipyl aminoacyl l-d isomerisation, a peculiar and subtle posttranslational modification.

  3. Research Articles

    1. Top of page
    2. Issue Information
    3. Review
    4. Research Articles
    1. Evaluation of in vitro properties of predicted kinases that phosphorylate serine residues within nuclear localization signal 1 of high mobility group box 1 (pages 613–617)

      Junichi Taira and Yuichiro Higashimoto

      Version of Record online: 25 MAY 2014 | DOI: 10.1002/psc.2630

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      Two nuclear localization signals (NLSs), NLS1 and NLS2, in high mobility group box 1 (HMGB1) regulate its nucleocytoplasmic relocation, and phosphorylation of both NLSs promotes HMGB1 mobilization. In the present study, kinases that phosphorylate serine residues within NLS1 were predicted, and an in vitro kinase assay was performed. Among the predicted kinases, protein kinase C phosphorylated Ser46 of HMGB1-derived peptides and a mutagenesis experiment showed that this phosphorylation could induce translocation of the N-terminal region of HMGB1 to the cytosol.

    2. Ornithokinin (avian bradykinin) from the skin of the Chinese bamboo odorous frog, Odorrana versabilis (pages 618–624)

      Peng Lyu, Lilin Ge, Lei Wang, Xiaoxiao Guo, Huiling Zhang, Yihan Li, Yu Zhou, Mei Zhou, Tianbao Chen and Chris Shaw

      Version of Record online: 28 APR 2014 | DOI: 10.1002/psc.2631

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      An ornithokinin-encoding precursor protein was cloned form the skin secretion of the Chinese bamboo odorous frog, Odorrana versabilis. Its structure was consistent with a typical amphibian skin peptide precursor and was quite different from chicken ornithokininogen.

    3. Cationic heterooligopeptides by ficain-catalyzed co-oligomerization of lysine and methionine ethylesters (pages 625–629)

      Markus Andre, Boris Kühl, Gerald Brenner-Weiss, Christoph Syldatk and Jens Rudat

      Version of Record online: 9 MAY 2014 | DOI: 10.1002/psc.2639

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      The present study reports the ficain-catalyzed heterooligomerizations of H-Lys-OEt with H-Met-OEt. MALDI-ToF/ToF-MS analyses proved successful syntheses of cationic heterooligopeptides with a degree of polymerization between 7 and 10 amino acid residues, with the enzyme exhibiting a clear preference for methionine.

    4. Biodegradable delivery system containing a peptide inhibitor of polyglutamine aggregation: a step toward therapeutic development in Huntington's disease (pages 630–639)

      Abhayraj S. Joshi and Ashwani Kumar Thakur

      Version of Record online: 2 MAY 2014 | DOI: 10.1002/psc.2640

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      The nanoparticulate drug-delivery system was developed for a novel peptide inhibitor ‘PGQ9[P2]’. The in vitro characterization confirmed uniform and narrow distribution of particles below 200 nm with high entrapment of peptide. When PGQ9[P2]-loaded nanoparticles were incubated with aggregating peptide Q35P10 that represents N-terminus of Huntingtin, the released PGQ9[P2] suppressed its aggregation. These results indicate a progressive step toward the delivery of peptide inhibitor for therapeutic development in Huntington's disease.

    5. Antiplasmodial activity study of angiotensin II via Ala scan analogs (pages 640–648)

      Adriana Farias Silva, Erick Leite Bastos, Marcelo Der Torossian Torres, André Luis Costa-da-Silva, Rafaella Sayuri Ioshino, Margareth Lara Capurro, Flávio Lopes Alves, Antonio Miranda, Renata de Freitas Fischer Vieira and Vani Xavier Oliveira Jr.

      Version of Record online: 9 MAY 2014 | DOI: 10.1002/psc.2641

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      Aiming to understand the residue relevance on angiotensin II antiplasmodial activity in Plasmodium gallinaceum sporozoites, it was performed an Ala scan study, in which the importance of Arg2, Tyr4, Pro7, and Phe8 side chains was noticed by fluorescence microscopy. The results obtained with these analogs showed that hydrophobic cluster and van der Waals interactions preservation are of utmost consideration to this class of peptides. The β-turn conformations of the most active analogs were verified by circular dichroism studies.

    6. Dissecting a role of a charge and conformation of Tat2 peptide in allosteric regulation of 20S proteasome (pages 649–656)

      Julia Witkowska, Przemysław Karpowicz, Maria Gaczynska, Pawel A. Osmulski and Elżbieta Jankowska

      Version of Record online: 13 MAY 2014 | DOI: 10.1002/psc.2642

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      Ala scan studies of Tat2 peptide, a noncompetitive inhibitor of human SDS-activated 20S proteasome and a weak activator of the latent 20S, revealed that different peptide features are responsible for its stimulating and inhibitory activity toward the proteasome chymotrypsin-like peptidase. While for stimulating capacity preservation of the PPII/turn conformation seems to play an important role, inhibitory capacity depends rather on the positive charge.

    7. Large scale conformational transitions in β-structural motif of gramicidin A: kinetic analysis based on CD and FT-IR data (pages 657–667)

      Sergei V. Sychev and Vadim T. Ivanov

      Version of Record online: 2 MAY 2014 | DOI: 10.1002/psc.2643

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      Transfer of Cs-gA complex into the TX-100 micelles and dioxane solution activates a cascade of sequential conformational transitions monitored by CD and FT-IR spectroscopy. Kinetics of the transitions was measured and the activation parameters determined. The results are discussed in the light of local unfolding, (or “cracking”) model of large scale conformational transitions.

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