Journal of Peptide Science

Cover image for Vol. 19 Issue 4

Special Issue: Special issue devoted to contributions presented at the 13th Naples Workshop on Bioactive Peptides, June 7–10, 2012, Naples

April 2013

Volume 19, Issue 4

Pages 181–262

Issue edited by: Giancarlo Morelli

  1. Editorial

    1. Top of page
    2. Editorial
    3. Special Issue Articles
  2. Special Issue Articles

    1. Top of page
    2. Editorial
    3. Special Issue Articles
    1. Quantifying molecular partition of cell-penetrating peptide–cargo supramolecular complexes into lipid membranes: optimizing peptide-based drug delivery systems (pages 182–189)

      João Miguel Freire, Ana Salomé Veiga, Beatriz G. de la Torre, David Andreu and Miguel A. R. B. Castanho

      Version of Record online: 16 JAN 2013 | DOI: 10.1002/psc.2477

      Thumbnail image of graphical abstract

      This methodology allows the determination of the membrane partition constant (KP,C) of the cell penetrating peptide (CPP)–cargo complex. It considers a concomitant double partition (involving both free CPP, Kp, and the CPP–cargo complexes, KP,C) and aqueous binding equilibrium between CPP and the cargo, responsible for the complex formation – Kb.

    2. Octreotide labeled aggregates containing platinum complexes as nanovectors for drug delivery (pages 190–197)

      Antonella Accardo, Gaetano Mangiapia, Luigi Paduano, Giancarlo Morelli and Diego Tesauro

      Version of Record online: 25 JAN 2013 | DOI: 10.1002/psc.2481

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      New liposomal aggregates obtained by co-assembling an amphiphilic molecule containing a platinum complex, with a second amphiphilic monomer containing the octreotide bioactive peptide, are described.

      The obtained liposomes could represent a new target selective cargo system for delivery of cisplatin based drugs and/or doxorubicin on cells overexpressing the sstr2 and sstr5 somatostatin receptors.

    3. Nanoparticles exposing neurotensin tumor-specific drivers (pages 198–204)

      Chiara Falciani, Jlenia Brunetti, Barbara Lelli, Antonella Accardo, Diego Tesauro, Giancarlo Morelli and Luisa Bracci

      Version of Record online: 25 FEB 2013 | DOI: 10.1002/psc.2493

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      Branched-neurotensin peptides have the ability to drive liposomes to target cells and deliver their toxic cargo. We show here that the more densely decorated liposomes had a better activity profile in terms of drug delivery.

    4. Biodegradable paclitaxel-loaded microparticles prepared from novel block copolymers: influence of polymer composition on drug encapsulation and release (pages 205–213)

      Susanna Sartori, Andrea Caporale, Alfonsina Rechichi, Domenico Cufari, Caterina Cristallini, Niccoletta Barbani, Paolo Giusti and Gianluca Ciardelli

      Version of Record online: 12 MAR 2013 | DOI: 10.1002/psc.2491

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      Degradable block copolymers were designed for use in advanced drug delivery systems. Copolymers where synthesised and used as carriers for the controlled delivery of an antineoplastic drug. Chromatographic analysis demonstrated that the drug release can be fine-tuned by changing the polymer composition. Particles of a polyurethane further functionalised with the RGD sequence were realised in order to obtain a target DDS.

    5. Structural investigation of the VEGF receptor interaction with a helical antagonist peptide (pages 214–219)

      Donatella Diana, Rossella Di Stasi, Lucia De Rosa, Carla Isernia, Luca D. D'Andrea and Roberto Fattorusso

      Version of Record online: 19 FEB 2013 | DOI: 10.1002/psc.2480

      Thumbnail image of graphical abstract

      Recently, the designed peptide, named MA, has been demonstrated to assume in water a well-defined helical conformation, to bind to vascular endothelial growth factor (VEGF) receptors, and to inhibit the VEGF-induced capillary formation and tumor growth. In this study, we identified, combining solution NMR studies and molecular modeling, the molecular determinants of the binding surface between peptide MA and VEGFR1D2. Particularly, the peptide binding site on VEGFR1D2 and peptide residues involved in receptor recognition have been determined.

    6. Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide (pages 220–226)

      Maria Stefania Spagnuolo, Rossella Di Stasi, Lucia De Rosa, Bernadetta Maresca, Luisa Cigliano and Luca D. D'Andrea

      Version of Record online: 19 FEB 2013 | DOI: 10.1002/psc.2487

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      The molecular determinants underlining the interaction between Hpt and the ApoA-I-derived P2a peptide were investigated deleting terminal regions and replacing conserved residues with alanine. P2a analogs presenting E146A or D157A substitutions showed a better biological activity than P2a peptide.

    7. Interaction of cisplatin with a CCHC zinc finger motif (pages 227–232)

      Maria Antonietta Castiglione Morelli, Angela Ostuni, Pier Luigi Cristinziano, Diego Tesauro and Alfonso Bavoso

      Version of Record online: 19 FEB 2013 | DOI: 10.1002/psc.2490

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      This study is focused on the interaction between cisplatin and an 18-residue CCHC zinc finger motif derived from a retroviral nucleocapsid protein (PyrZf18) UV–visible, CD and 1H NMR spectroscopies and ESI-MS spectrometry.

      The results are discussed with respect to the potential antiretroviral activity of platinum(II) compounds and to the possible interaction of cisplatin with the cellular nucleic acid binding proteins.

    8. Antinociceptive profile of potent opioid peptide AM94, a fluorinated analogue of biphalin with non-hydrazine linker (pages 233–239)

      Adriano Mollica, Roberto Costante, Azzurra Stefanucci, Francesco Pinnen, Gino Lucente, Stefano Fidanza and Stefano Pieretti

      Version of Record online: 8 NOV 2012 | DOI: 10.1002/psc.2465

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      The antinociceptive profile of AM94 has been evaluated by in vivo nociception tests, in rats (tail flick test) and in mice (formalin test). Result have been compared with those of biphalin and morphine. Variable-temperature 1H NMR experiments and energy minimization were also carried out.

    9. Antimicrobial peptides from plants: stabilization of the γ core of a tomato defensin by intramolecular disulfide bond (pages 240–245)

      C. Avitabile, R. Capparelli, M. M. Rigano, A. Fulgione, A. Barone, C. Pedone and A. Romanelli

      Version of Record online: 19 FEB 2013 | DOI: 10.1002/psc.2479

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      Oxidation of a plant defensin fragment results in a boomerang-like structure, in which positive charges necessary for the interaction with the negatively charged lipopolysaccharide (LPS) are exposed.

    10. Spectroscopically labeled peptaibiotic analogs: the 4-nitrophenylalanine infrared absorption probe inserted at different positions into trichogin GA IV (pages 246–256)

      Cristina Peggion, Barbara Biondi, Marta De Zotti, Simona Oancea, Fernando Formaggio and Claudio Toniolo

      Version of Record online: 27 DEC 2012 | DOI: 10.1002/psc.2475

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      In this work, we synthesized and extensively characterized three analogs of the lipopeptaibiotic trichogin GA IV, mono-labeled with the IR absorption probe Phe(NO2) at different positions in the amino acid sequence. These analogs preserve the helical conformation, membrane-modifying properties, and in vitro antibacterial activities of the native compound. However, from our IR absorption and attenuated total reflectance IR experiments, the nitrobenzyl probe seems not to be a particularly environment-sensitive reporter group.

    11. C-terminus of ET A/ETB receptors regulate endothelin-1 signal transmission (pages 257–262)

      Achani Yatawara, Jamie L. Wilson, Linda Taylor, Peter Polgar and Dale F. Mierke

      Version of Record online: 25 FEB 2013 | DOI: 10.1002/psc.2499

      Thumbnail image of graphical abstract

      A cytoplasmic view of the binding of a helix from the C-terminus of the endothelin B receptor (residues Y430–S442, shown in yellow) with the endothelin A receptor (surface representation, colored by hydrophobicity). Within the model, the helical peptide from ETB binds between the helical domains of the C-terminus and IC2 of the ETA receptor.

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