Journal of Peptide Science

Cover image for Vol. 18 Issue 9

September 2012

Volume 18, Issue 9

Pages 541–598

  1. Research Articles

    1. Top of page
    2. Research Articles
    1. The preparation of a complex of insulin–phospholipids and their interaction mechanism (pages 541–548)

      Cuiping Zhou, Xuejun Xia, Yuling Liu and Lin Li

      Version of Record online: 25 JUL 2012 | DOI: 10.1002/psc.2423

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      In this paper, we developed a novel technique to fabricate the insulin-phospholipids complex. The associated efficiency of the phospholipids and insulin can be up to 100% when their mol ratio is 49 : 1. The interaction mechanism of this formation is that the peptide bonds of insulin interact with the water-soluble head of phospholipids, forming a reverse micelle-like structure.

    2. A slow gradient approach for the purification of synthetic polypeptides by reversed phase high performance liquid chromatography (pages 549–555)

      Paul W.R. Harris, Dong Jun Lee and Margaret A. Brimble

      Version of Record online: 25 JUL 2012 | DOI: 10.1002/psc.2432

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      We illustrate a purification protocol using slow gradient chromatography that permits up to 900 mg of crude peptide to be purified in a single chromatographic step on semi-preparative reversed phase column resulting in high purities and good recoveries.

    3. TAPP analogs containing β3-homo-amino acids: synthesis and receptor binding (pages 556–559)

      D. Podwysocka, P. Kosson, A. W. Lipkowski and A. Olma

      Version of Record online: 12 JUL 2012 | DOI: 10.1002/psc.2433

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      α,β-Hybrids of Tyr- d-Ala-Phe-Phe-NH2 analogs were synthesized and tested for affinity to μ-opioid and δ-opioid receptors. Each amino acid was replaced with an l- or d3-h-amino acid. The analog Tyr-β3h- d-Ala-Phe-PheNH2 was found to be slightly more active than the native tetrapeptide. It may adopt a conformation well tolerated by the μ-opioid receptor during the peptide ligand–receptor interaction.

    4. Synthesis, biological activity and conformational analysis of head-to-tail cyclic analogues of LL37 and histatin 5 (pages 560–566)

      Elżbieta Kamysz, Emilia Sikorska, Anna Karafova and Małgorzata Dawgul

      Version of Record online: 12 JUL 2012 | DOI: 10.1002/psc.2434

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      This paper describes the synthesis and structure-activity studies of head-to-tail cyclic analogues of LL37 and histatin 5. An innovative application of microwave technology to cleavage a protected peptide from the 2-chlorotrityl chloride resin has been implemented.

    5. Synthesis of short cationic antimicrobial peptidomimetics containing arginine analogues (pages 567–578)

      Leonardo Baldassarre, Francesco Pinnen, Catia Cornacchia, Erika Fornasari, Luigina Cellini, Marina Baffoni and Ivana Cacciatore

      Version of Record online: 17 JUL 2012 | DOI: 10.1002/psc.2435

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      Synthesis and antimicrobial activity of novels peptidomimetics containing arginine analogs have been reported. The biological screening showed that peptidomimetics 1–2 and 5–6 are endowed with the best antimicrobial activity against Staphylococcus aureus and Staphylococcus epidermidis. Moreover, peptidomimetics 2 and 5 showed an appreciable activity against the tested Gram-negative bacteria and Candida albicans.

    6. Improving membrane binding as a design strategy for amphipathic peptide hormones: 2-helix variants of PYY3-36 (pages 579–587)

      Søren L. Pedersen, Vikram K. Bhatia, Simon Jurt, Johan F. Paulsson, Maria H. Pedersen, Rasmus Jorgensen, Birgitte Holst, Dimitrios Stamou, Niels Vrang, Oliver Zerbe and Knud J. Jensen

      Version of Record online: 1 AUG 2012 | DOI: 10.1002/psc.2436

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      A radically redesigned 2-helix PYY3-36 analog shows improved membrane binding yet has a high receptor affinity.

    7. Synthesis and properties of cyclic gomesin and analogues (pages 588–598)

      Alessandra Machado, Marcos A. Fázio, Antonio Miranda, Sirlei Daffre and M. Teresa Machini

      Version of Record online: 1 AUG 2012 | DOI: 10.1002/psc.2439

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      The present study expands the knowledge on chemical peptide synthesis and on SAR of gomesin (Gm), an antimicrobial β-hairpin disulfide-stabilized peptide. The results prove the efficiency of our protocols at 60 °C using conventional heating for fast backbone cyclization and show that, although the insertion of such conformational constraint did not dramatically enhance antimicrobial activity or serum stability of Gm and its analogues, it led to selectivity and, in some cases, higher hemolytic activity and salt tolerance.

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