Journal of Peptide Science

Cover image for Vol. 18 Issue 7

July 2012

Volume 18, Issue 7

Pages 427–486

  1. Editorials

    1. Top of page
    2. Editorials
    3. Reviews
    4. Research Articles
  2. Reviews

    1. Top of page
    2. Editorials
    3. Reviews
    4. Research Articles
    1. Through the looking glass – a new world of proteins enabled by chemical synthesis (pages 428–436)

      Stephen Kent, Youhei Sohma, Suhuai Liu, Duhee Bang, Brad Pentelute and Kalyaneswar Mandal

      Article first published online: 4 JUN 2012 | DOI: 10.1002/psc.2421

      Thumbnail image of graphical abstract

      Total synthesis of proteins by modern chemical ligation methods has enabled the routine use of mirror-image protein molecules in structural biology as well as the synthesis of crystalline protein molecules with full enzymatic activity. A practical total chemical synthesis of insulin has been achieved via a key ester-linked protein molecule of novel topology. Racemic protein crystallography has enabled the determination of X-ray structures of recalcitrant protein molecules.

    2. Peptides as asymmetric catalysts and templates for the controlled formation of Ag nanoparticles (pages 437–441)

      Helma Wennemers

      Article first published online: 31 MAY 2012 | DOI: 10.1002/psc.2422

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      Research in the Wennemers group focuses on the development of small molecules for functions that are fulfilled in nature by large macromolecules. The Zervas Award presentation focused on the use of tripeptides of the type H-Pro-Pro-Xaa as asymmetric catalysts and short peptides as templates for the controlled formation of silver nanoparticles.

  3. Research Articles

    1. Top of page
    2. Editorials
    3. Reviews
    4. Research Articles
    1. Cysteine racemization during the Fmoc solid phase peptide synthesis of the Nav1.7-selective peptide – protoxin II (pages 442–448)

      Jae H. Park, Kevin P. Carlin, Gang Wu, Victor I. Ilyin and Donald J. Kyle

      Article first published online: 17 MAY 2012 | DOI: 10.1002/psc.2407

      Thumbnail image of graphical abstract

      HPLC trace of crude linear protoxin II. Other eight toxins gave similar HPLC trace

    2. Structural insights into the transmembrane domains of human copper transporter 1 (pages 449–455)

      Lei Yang, Zhaowei Huang and Fei Li

      Article first published online: 21 MAY 2012 | DOI: 10.1002/psc.2415

      Thumbnail image of graphical abstract

      The structures of the transmembrane segments of hCtr1 in HFIP aqueous solution studied by solution NMR were reported firstly. It was revealed that TMD1 forms an α-helix from Gly67 to Glu84, TMD2 forms an amphiphilic α-helix spanning over Leu134-Thr155, whereas TMD3 adopts a discontinuous helix structure, known as ‘α-helix-coiled segment-α-helix’. The differences in the structures of the TMD peptides may be related to their different roles in the channel formation and transport function.

    3. Dimeric analogs of immunosuppressive decapeptide fragment of ubiquitin (pages 456–465)

      Alicja Kluczyk, Marzena Cydzik, Monika Biernat, Remigiusz Bąchor, Paweł Pasikowski, Piotr Stefanowicz, Jolanta Artym, Michał Zimecki and Zbigniew Szewczuk

      Article first published online: 25 MAY 2012 | DOI: 10.1002/psc.2416

      Thumbnail image of graphical abstract

      Three dimerization strategies via PEG derivatives were used to synthesize the analogs of LEDGRTLSDY ubiquitin fragment on solid support. The immunological tests showed that the head-to-tail dimerization causes a more profound increase in the biological activity than other tested dimerization methods.

    4. Conformations of helical Aib peptides containing a pair of l-amino acid and d-amino acid (pages 466–475)

      Yosuke Demizu, Yu-u Yabuki, Mitsunobu Doi, Yukiko Sato, Masakazu Tanaka and Masaaki Kurihara

      Article first published online: 22 MAY 2012 | DOI: 10.1002/psc.2418

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      A pair of l-Leu and d-Leu was incorporated into Aib peptide segments, and the conformations of their peptides were studied in solution and in the crystalline state.

    5. Designed synthetic analogs of the α-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin αvβ3 homing domain (pages 476–486)

      Yuwen Diao, Wenyu Han, Honglei Zhao, Seng Zhu, Xiaohe Liu, Xin Feng, Jingmin Gu, Cuimei Yao, Shanshan Liu, Changjiang Sun and Fengguang Pan

      Article first published online: 28 MAY 2012 | DOI: 10.1002/psc.2420

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      RGD-Las containing two functional domains, the RGD tripeptide and charge-modified Temporin-La analogs, was shown to be highly selective against αvβ3-positive tumor cells with the net negative surface charges. The new active chimera peptides have clinical potential as specifically targeted anticancer agents.

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