Journal of Peptide Science

Cover image for Vol. 17 Issue 3

March 2011

Volume 17, Issue 3

Pages 169–232

  1. Protocols

    1. Top of page
    2. Protocols
    3. Research Articles
    1. General method for selective labelling of double-chain cysteine-rich peptides with a lanthanide chelate via solid-phase synthesis (pages 169–173)

      Fazel Shabanpoor, Frances Separovic and John D. Wade

      Article first published online: 11 JAN 2011 | DOI: 10.1002/psc.1307

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      Use of a suitably derivatized DTPA chelate for acylation at the N-terminus of a solid phase assembled and bound peptide allows the subsequent ready and simple preparation of an insulin-like peptide via sequential formation of three disulfide bonds and formation of complex between DTPA and europium using excess EuCl3. The resulting labeled peptide displays femtomolar fluorescence detection sensitivity making it an attractive alternative to radiolabeled analogues for high throughput receptor binding screening.

  2. Research Articles

    1. Top of page
    2. Protocols
    3. Research Articles
    1. Conformational space search of Neuromedin C using replica exchange molecular dynamics and molecular dynamics (pages 174–183)

      Parul Sharma, Parvesh Singh, Krishna Bisetty, Alex Rodriguez and Juan J. Perez

      Article first published online: 27 SEP 2010 | DOI: 10.1002/psc.1295

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      Multicanonical Replica Exchange molecular dynamics (REMD) along with standard molecular dynamics (MD) techniques are employed to explore the conformational space of Neuromedin C under implicit and explicit solvent conditions. REMD in explicit solvent appears to be more efficient in sampling new conformations, and promotes a greater number of beta turns and bent structures, while the others preferably generate helices in the structures. REMD performed under explicit solvent conditions show good agreement with the experimental NMR results in the presence of Ni(II).

    2. Epitope motif of an anti-nitrotyrosine antibody specific for tyrosine-nitrated peptides revealed by a combination of affinity approaches and mass spectrometry (pages 184–191)

      Mihaela Drǎguşanu, Brînduşa-Alina Petre and Michael Przybylski

      Article first published online: 11 JAN 2011 | DOI: 10.1002/psc.1298

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      The affinity of tyrosine nitrated peptides to a specific anti-3-nitrotyrosine antibody depends not merely on a single nitrated tyrosine residue, but is shown to comprise an epitope motif with positively charged neighbouring amino acids (Lys and/or Arg) N-terminal to the tyrosine nitration site. High antibody binding was found with basic (Lys, Arg) amino acids located at a distance of 2-3 amino acid residues from the nitrated tyrosine.

    3. The action of fish peptide Orpotrin analogs on microcirculation (pages 192–199)

      Katia Conceição, Fernanda Miriane Bruni, Juliane M. Santos, Robson Melo Lopes, Elineide E. Marques, Jorge H. Fernandez and Mônica Lopes-Ferreira

      Article first published online: 23 NOV 2010 | DOI: 10.1002/psc.1311

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      We have evaluated the molecular modeling, dynamics and effects of three Orpotrin analogues (Orp-desH1, Orp-Nle, and Orp-Pro/Ala) in microcirculation by intravital microscopy. Our results showed that only Orp-desH1, could induce vasoconstriction effect, indicating that the positive charge for lysine and the proline residue is crucial for this vasoconstriction effect. In addition, this study has demonstrated that even subtle changes on the primary structure of Orpotrin alter significantly the biological effects of this native peptide, which could be of interest for biotechnological purposes.

    4. Analysis of the interacting surface of maurotoxin with the voltage-gated Shaker B K+ channel (pages 200–210)

      Ziad Fajloun, Nicolas Andreotti, Mohamed Fathallah, Jean-Marc Sabatier and Michel De Waard

      Article first published online: 11 JAN 2011 | DOI: 10.1002/psc.1313

      Maurotoxin (MTX) is a 34-residue toxin that was isolated initially from the venom of the scorpion Scorpio maurus palmatus. Unlike the other toxins of the α-KTx6 family (Pi1, Pi4, Pi7, and HsTx1), MTX exhibits a unique disulfide bridge organization of the type C1[BOND]C5, C2[BOND]C6, C3[BOND]C4, and C7[BOND]C8 (instead of the conventional C1[BOND]C5, C2[BOND]C6, C3[BOND]C7, and C4[BOND]C8, herein referred to as Pi1-like) that does not prevent its folding along the classic α/β scaffold of scorpion toxins. MTXPi1 is an MTX variant with a conventional pattern of disulfide bridging without any primary structure alteration of the toxin.

    5. Synthesis, biological activity and solution structure of new analogues of the antimicrobial Gramicidin S (pages 211–217)

      Elżbieta Kamysz, Beata Mickiewicz, Wojciech Kamysz, Sylwia Bielińska, Sylwia Rodziewicz-Motowidło and Jerzy Ciarkowski

      Article first published online: 25 OCT 2010 | DOI: 10.1002/psc.1314

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      The work describes the synthesis, antimicrobial and hemolytic activities as well as solution structures of three new analogues of Gramicidin S designed with the purpose of perturbing their amphipathic moments. A novel approach to the synthesis of head-to-tail cyclopeptides has been presented.

    6. You have free access to this content
      Charge inversion at position 68 of the glucagon and glucagon-like peptide-1 receptors supports selectivity in hormone action (pages 218–225)

      Jonathan W. Day, Pengyun Li, James T. Patterson, Joe Chabenne, Maria DiMarchi Chabenne, Vasily M. Gelfanov and Richard D. DiMarchi

      Article first published online: 30 NOV 2010 | DOI: 10.1002/psc.1317

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      The activity of a structurally diverse set of glucagon-like peptides was assessed at the GLP-1 receptor and two related single site mutants. This study reveals that single amino acid differences at positions 68 & 128 in GLP-1R influence selectivity for ligand action.

    7. Influenza virus H5N1 hemagglutinin (HA) T-cell epitope conjugates: design, synthesis and immunogenicity (pages 226–232)

      Theodore Skarlas, Stella Zevgiti, Karoline Droebner, Eugenia Panou-Pomonis, Oliver Planz and Maria Sakarellos-Daitsiotis

      Article first published online: 30 NOV 2010 | DOI: 10.1002/psc.1320

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      A reconstituted mimic of the H5 HA antigen was formulated by chemoselective ligation of H5 HA T-cell epitopes to an artificial carrier SOC4 for evaluation of its immunogenicity.