Journal of Peptide Science

Cover image for Vol. 17 Issue 7

July 2011

Volume 17, Issue 7

Pages 487–544

  1. Research Articles

    1. Top of page
    2. Research Articles
    1. Peptide synthesis ‘in water’ by a solution-phase method using water-dispersible nanoparticle Boc-amino acid (pages 487–492)

      Keiko Hojo, Hideki Ichikawa, Mare Onishi, Yoshinobu Fukumori and Koichi Kawasaki

      Article first published online: 14 APR 2011 | DOI: 10.1002/psc.1367

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      Regulatory pressure has compelled the chemical manufacturing industry to reduce the use of organic solvents in synthetic chemistry, and there is currently a strong focus on replacing these solvents with water. Here, we describe an efficient in-water solution-phase peptide synthesis method using Boc-amino acids. It is based on a coupling reaction utilizing suspended waterdispersible nanoparticle reactants. Using this method, peptides were obtained in good yield and with high purity.

    2. Characterization of antilytic peptide antibody: application for the detection of lytic-based hybrid peptide in serum samples (pages 493–498)

      Koji Ohara, Tomohisa Horibe, Masayuki Kohno and Koji Kawakami

      Article first published online: 24 FEB 2011 | DOI: 10.1002/psc.1349

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      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. Protective effect of recombinant human glucagon-like peptide-1 (rhGLP-1) pretreatment in STZ-induced diabetic mice (pages 499–504)

      Ye-Lin Wu, Jing Huang, Jian Liu, Ming-Fei Jin, Mei Gu, Yiguo Hong and Zi-Rong Wu

      Article first published online: 14 APR 2011 | DOI: 10.1002/psc.1352

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      In this paper, we found rhGLP-1 pretreatment has a protective effect against STZ-induced diabetes in mice. Pretratment of rhGLP-1 not only decreased blood glucose and improved glucose tolerance but also significantly reduced the level of oxidative stress and elevated the antioxidant defense system activities in STZ-induced diabetic mouse model. These findings suggest that GLP-1 and its analogs may be a new therapeutic strategy in the preventive and protective treatment of diabetes mellitus.

    4. Folding and assembly of TMD 6-related segments of DMT 1 in trifluoroethanol aqueous solution (pages 505–511)

      Shuyan Xiao, Chunyu Wang, Jiantao Li and Fei Li

      Article first published online: 24 FEB 2011 | DOI: 10.1002/psc.1356

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      DMT1-TMD6 forms a discontinuous helix structure in TFE aqueous solution. The H267A mutation decreases the length of the linker, while the H272A mutation extends it. These peptides aggregate as trimers with different intermolecular affinity.

    5. Silver-induced conformational changes of polypeptides: a CD study (pages 512–519)

      Manuela Murariu, Ecaterina Stela Dragan, Adriana Adochitei, Gheorghita Zbancioc and Gabi Drochioiu

      Article first published online: 28 APR 2011 | DOI: 10.1002/psc.1359

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      The glycine-based, histidine-containing peptide showed a severe change from a random coil and β-turn conformation to large α-helices during silver binding. When comparing the effect of silver ions on the conformation of bradykinin a similar tendency was found. Besides, silver ions reduced the amyloid-β peptide tendency to aggregation.

    6. Cell selectivity and interaction with model membranes of Val/Arg-rich peptides (pages 520–526)

      Qing-Quan Ma, An-Shan Shan, Na Dong, Yao Gu, Wen-Yu Sun, Wan-Ning Hu and Xing-Jun Feng

      Article first published online: 22 MAR 2011 | DOI: 10.1002/psc.1360

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      The peptides were produced by segregating hydrophilic residues on the polar side and hydrophobic residues on the opposite side. The peptides displayed strong antimicrobial activity against Gram-negative and Gram-positive bacteria, but weak haemolysis. The peptides bound preferentially to negatively charged phospholipids over zwitterionic phospholipids, which correspond well with the biological activity data.

    7. Synthesis of the orthogonally protected amino alcohol Phaol and analogs (pages 527–532)

      Jo Nelissen, Koen Nuyts, Wim Dehaen and Wim M. De Borggraeve

      Article first published online: 14 APR 2011 | DOI: 10.1002/psc.1362

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      The development of a multigram synthesis of the orthogonally protected amino acid-derived Phaol [2-{[(2S)-2-amino-3-phenylpropyl]amino}ethanol] is described, two synthetic schemes were proposed and examined. Between the reduction-coupling and the coupling-reduction scheme, the latter gave the best results. This two-step synthesis affords easily purifiable products and several analogs were synthesized.

    8. Synthesis and biological evaluation of analogues of the marine cyclic depsipeptide obyanamide (pages 533–539)

      Wei Zhang, Ning Ding and Yingxia Li

      Article first published online: 14 APR 2011 | DOI: 10.1002/psc.1361

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      The preparation and preliminary cytotoxicities evaluation of obyanamide analogues with different substitutions and configurations in the building blocks were reported.

    9. A defensin-like antimicrobial peptide from the venoms of spider, Ornithoctonus hainana (pages 540–544)

      Hongwen Zhao, Yi Kong, Hanjin Wang, Tianhua Yan, Feifei Feng, Jianmin Bian, Yan Yang and Haining Yu

      Article first published online: 28 APR 2011 | DOI: 10.1002/psc.1370

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      A defensin-like antimicrobial peptide named Oh-defensin was purified and characterized from the venoms of the spider, Ornithoctonus hainana. Oh-defensin is composed of 52 amino acid residues including 6 cysteines that possibly form three disulfide bridges. Oh-defensin showed significant sequence similarity to other arthropod antimicrobial peptides of the defensin family. Oh-defensin exerted potent antimicrobial activities against tested microorganisms including Gram-positive bacteria, Gram-negative bacteria and fungi.