Journal of Peptide Science

Cover image for Vol. 17 Issue 5

Special Issue: Peptides at work: from structure to applications

May 2011

Volume 17, Issue 5

Pages 297–412

Issue edited by: Ettore Benedetti, Kyung-Soo Hahm, Lorenzo Stella

  1. Editorial

    1. Top of page
    2. Editorial
    3. Reviews
    4. Research Articles
    1. Peptides at work: from structure to applications (page 297)

      Ettore Benedetti, Kyung-soo Hahm and Lorenzo Stella

      Version of Record online: 7 APR 2011 | DOI: 10.1002/psc.1373

  2. Reviews

    1. Top of page
    2. Editorial
    3. Reviews
    4. Research Articles
    1. Bacterial membrane lipids in the action of antimicrobial agents (pages 298–305)

      Richard M. Epand and Raquel F. Epand

      Version of Record online: 30 NOV 2010 | DOI: 10.1002/psc.1319

      Thumbnail image of graphical abstract

      A mechanism contributing to the antimicrobial action of certain agents is illustrated. The effect is a consequence of rearrangements of the bacterial membrane as a consequence of the interaction of a polycationic peptide (blue) selectively interacting with anionic lipid components (red) in the membrane and causing these lipids to cluster in a separate region of the membrane.

    2. Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations (pages 306–314)

      Burkhard Bechinger

      Version of Record online: 28 FEB 2011 | DOI: 10.1002/psc.1343

      Thumbnail image of graphical abstract

      Biophysical investigations of linear cationic antimicrobial peptides are indicative that these amphipathic molecules orient parallel to the surface of membranes that represent well the lipid composition of bacteria or eukaryotes. Here such data are reviewed and discussed in terms of the various models hat have been suggested to explain the biological activities of magainins and related peptides.

      Corrected by:

      Erratum: Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations

      Vol. 21, Issue 8, 689, Version of Record online: 22 JUL 2015

    3. Probing structural transitions in both structured and disordered proteins using site-directed spin-labeling EPR spectroscopy (pages 315–328)

      Sonia Longhi, Valérie Belle, André Fournel, Bruno Guigliarelli and Frédéric Carrière

      Version of Record online: 24 FEB 2011 | DOI: 10.1002/psc.1344

      Thumbnail image of graphical abstract

      In this review we briefly describe the theoretical principles of site-directed spin-labeling EPR spectroscopy and illustrate how we successfully applied it to investigate structural transitions in both human pancreatic lipase (HPL), a well-folded protein, and within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein (NTAIL) upon addition of ligands and/or protein partners.

  3. Research Articles

    1. Top of page
    2. Editorial
    3. Reviews
    4. Research Articles
    1. Reversed sequence enhances antimicrobial activity of a synthetic peptide (pages 329–334)

      Ramamourthy Gopal, Young Jin Kim, Chang Ho Seo, Kyung-Soo Hahm and Yoonkyung Park

      Version of Record online: 1 APR 2011 | DOI: 10.1002/psc.1369

      Thumbnail image of graphical abstract

      The (KW)3 was noticed to be the reversed sequence of (WK)3. These studies found that a reversed peptide showed increased antimicrobial and membrane permeability activity than did normal peptide, while simultaneously maintaining their non-hemolytic activity.

    2. The thin line between cell-penetrating and antimicrobial peptides: the case of Pep-1 and Pep-1-K (pages 335–341)

      Sara Bobone, Alessandro Piazzon, Barbara Orioni, Jens Z. Pedersen, Yong Hai Nan, Kyung-Soo Hahm, Song Yub Shin and Lorenzo Stella

      Version of Record online: 4 FEB 2011 | DOI: 10.1002/psc.1340

      Thumbnail image of graphical abstract

      Antimicrobial and cell-penetrating peptides (AMPs and CPPs, respectively) are commonly considered two different classes of peptides, but here we show that three Glu to Lys substitutions in the sequence of a CPP can render it strongly bactericidal, due to its increased affinity for anionic membranes.

    3. Three novel antimicrobial peptides from the skin of the Indian bronzed frog Hylarana temporalis (Anura: Ranidae) (pages 342–347)

      V. Reshmy, V. Preeji, A. Parvin, K. Santhoshkumar and S. George

      Version of Record online: 15 MAR 2011 | DOI: 10.1002/psc.1363

      Thumbnail image of graphical abstract

      The present work describes the successful isolation of three novel peptides named brevinin-1TEa, brevinin-2TEa and brevinin-2TEb present in the skin secretion of Indian bronzed frog Hylarana temporalis.

    4. Peptides from Royal Jelly: studies on the antimicrobial activity of jelleins, jelleins analogs and synergy with temporins (pages 348–352)

      Alessandra Romanelli, Loredana Moggio, Rosa Chiara Montella, Pietro Campiglia, Marco Iannaccone, Federico Capuano, Carlo Pedone and Rosanna Capparelli

      Version of Record online: 19 JAN 2011 | DOI: 10.1002/psc.1316

      Thumbnail image of graphical abstract

      Peptides isolated from the Royal Jelly, the Jelleins, are mainly active against gram positive bacteria; interestingly they act in synergy with peptides belonging to the family of Temporins such as Temporin A and Temporin B.

    5. Effect of acidic pH on antibacterial action of peptide isolated from Korean pen shell (Atrina pectinata) (pages 353–357)

      Suyeon Yoo, Jin-Young Kim, Seong-Cheol Park, Do Young Choi, Chang Ho Seo, Kyung-Soo Hahm and Yoonkyung Park

      Version of Record online: 4 APR 2011 | DOI: 10.1002/psc.1372

      Thumbnail image of graphical abstract

      An antibacterial peptide (KPS-1) with molecular weight of 4549.4 Da was isolated from Korean pen shell (Atrina pectinata) and its activity was pH-dependent against Gram-negative bacteria.

    6. Alanine scanning analysis and structure–function relationships of the frog-skin antimicrobial peptide temporin-1Ta (pages 358–365)

      Paolo Grieco, Vincenzo Luca, Luigia Auriemma, Alfonso Carotenuto, Maria Rosaria Saviello, Pietro Campiglia, Donatella Barra, Ettore Novellino and Maria Luisa Mangoni

      Version of Record online: 18 FEB 2011 | DOI: 10.1002/psc.1350

      Thumbnail image of graphical abstract

      Structure-activity studies of the antimicrobial peptide temporin-1Ta (FLPLIGRVLSGIL-NH2) were performed, by replacing each individual amino acid with alanine. This allowed to elucidate the contribution of the side chains of each amino acid and the critical positions within the peptide's sequence to govern the antimicrobial/hemolytic activities of temporin-1Ta. It was found that hydrophobicity is a key parameter to determine the peptides's biological activity.

    7. Novel analogues of bradykinin conformationally restricted in the C-terminal part of the molecule (pages 366–372)

      Małgorzata Śleszyńska, Tomasz H. Wierzba, Krzysztof Malinowski, Lenka Borovičková, Izabela Małuch, Dariusz Sobolewski, Bernard Lammek, Jiřina Slaninová and Adam Prahl

      Version of Record online: 15 MAR 2011 | DOI: 10.1002/psc.1351

      Thumbnail image of graphical abstract

      The present work describes the synthesis and some pharmacological properties of six new analogues of bradykinin designed by replacement of D-Phe at position 7 of the model B2 receptor antagonist (Stewart's antagonist [D-Arg0,Hyp3,Thi5, 8,D-Phe7]-BK) with N-(Bzl)-Gly (a), X1 (b) or X2 (c). The D-Phe7 substitution with the aforementioned residues led to suppression of antagonistic activity of the new peptides. However, these non-coded achiral amino acids are still acceptable at that position.

    8. Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: implications for KCTD—cullin 3 recognition (pages 373–376)

      Luciano Pirone, Stefania Correale, Ivan de Paola, Laura Zaccaro, Giuseppina De Simone, Luigi Vitagliano, Emilia Pedone and Sonia Di Gaetano

      Version of Record online: 24 MAR 2011 | DOI: 10.1002/psc.1366

      Thumbnail image of graphical abstract

      By using molecular modeling and literature mutagenesis analyses, we here designed and characterized a peptide that is able to interact with submicromolar affinities with KCTD11 and KCTD5, two members of the KCTD family. This finding suggests that the tetrameric KCTD11 and the pentameric KCTD5 are endowed with a similar cavity at the subunit-subunit interface deputed to the Cul3 binding, despite their different oligomeric state.

    9. Comparison of distance information in [TOAC1, Glu(OMe)7, 18, 19] alamethicin F50/5 from paramagnetic relaxation enhancement measurements with data obtained from an X-ray diffraction-based model (pages 377–382)

      Rani Alphonsa Jose, Marta De Zotti, Cristina Peggion, Fernando Formaggio, Claudio Toniolo and Wim M. De Borggraeve

      Version of Record online: 15 MAR 2011 | DOI: 10.1002/psc.1354

      Thumbnail image of graphical abstract

      Nitroxide to peptide NH proton distances, obtained from PRE studies on a [TOAC1]alamethicin analog, are compared with those derived from an X-ray diffraction-based model. The two sets of distances were found to be in close agreement.

    10. Discovery of potent, cyclic calcitonin gene-related peptide receptor antagonists (pages 383–386)

      Liang Zeng Yan, Kirk W. Johnson, Emily Rothstein, David Flora, Patrick Edwards, Baolin Li, Junqing Li, Renee Lynch, Renee Vaughn, Amy Clemens-Smith, Deborah McCarty, Charles Chow, Kevin L. McKnight, Jirong Lu, Eric S Nisenbaum and John P. Mayer

      Version of Record online: 15 MAR 2011 | DOI: 10.1002/psc.1358

      Thumbnail image of graphical abstract

      Calcitonin Gene-Related Peptide (CGRP), a potent dilator of cerebral vasculature is known to be elevated in plasma and cerebrospinal fluid during migraine attacks. Our efforts to develop CGRP antagonists focused on the C-terminal portion of the natural peptide ligand known to bind the receptor but lack agonist properties. Extensive SAR studies identified a novel cyclic structure: (4-fluoro-benzoyl)-(D-Val)-Tyr-cyclo[Cys-Dap-Asp-Val-Gly-Pro-Phe-Cys]-3Pal-NH2 (35) with a Kb value of 0.0491 nM against the cloned hCGRP1 receptor.

    11. Neuroglobin–prion protein interaction: what's the function? (pages 387–391)

      Pasquale Palladino, Giovanni Luca Scaglione, Alessandro Arcovito, Rosa Maria Vitale, Pietro Amodeo, Beatrice Vallone, Maurizio Brunori, Ettore Benedetti and Filomena Rossi

      Version of Record online: 4 FEB 2011 | DOI: 10.1002/psc.1333

      Thumbnail image of graphical abstract

      Neuroglobin, a heme-protein discovered in the nervous system of vertebrates, plays a role in neuroprotection with a still unclear mechanism. Recently, it was reported retinal co-localization of neuroglobin and cellular prion protein, also a protein of unknown function expressed in the nervous system. We have evaluated neuroglobin–prion protein association in vitro by surface plasmon resonance technique. A combined approach of automated docking and molecular dynamics studies carried out on short stretches of prion N-terminus have identified interacting regions with neuroglobin.

    12. Development of high-throughput phosphorylation profiling method for identification of Ser/Thr kinase specificity (pages 392–397)

      Eun-Mi Kim, Jaehi Kim, Yun-Gon Kim, Peter Lee, Dong-Sik Shin, Mira Kim, Ji-Sook Hahn, Yoon-Sik Lee and Byung-Gee Kim

      Version of Record online: 22 NOV 2010 | DOI: 10.1002/psc.1312

      Thumbnail image of graphical abstract

      Detection assay to determine Ser/Thr kinase substrate specificity. The bead that contained substrate peptide was selected using color change by reaction of AP.

    13. Desirability function combining metabolic stability and functionality of peptides (pages 398–404)

      Sylvia Van Dorpe, Antita Adriaens, Simon Vermeire, Ingeborgh Polis, Kathelijne Peremans and Bart De Spiegeleer

      Version of Record online: 4 FEB 2011 | DOI: 10.1002/psc.1323

      Thumbnail image of graphical abstract

      The blood–brain barrier (BBB) influx and efflux functionalities of peptides as well as the metabolic stability in plasma and brain are quantitatively combined into a desirability function. Such a multi-criteria decision method objectively reveals the best peptide drug candidate, which was confirmed by in vivo imaging experiments.

    14. Gastrin and cholecystokinin peptide-based radiopharmaceuticals: an in vivo and in vitro comparison (pages 405–412)

      Anna Lucia Tornesello, Michela Aurilio, Antonella Accardo, Laura Tarallo, Antonio Barbieri, Claudio Arra, Diego Tesauro, Giancarlo Morelli and Luigi Aloj

      Version of Record online: 24 FEB 2011 | DOI: 10.1002/psc.1327

      Thumbnail image of graphical abstract

      Among six different peptide conjugates investigated in vitro and in vivo, DOTA coupled CCK8 peptide provided the best tumor to kidney uptake ratio and appears more suitable as lead compound for improvement of radiopharmaceutical properties.

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