Journal of Peptide Science

Cover image for Journal of Peptide Science

May 2010

Volume 16, Issue 5

Pages 213–255

  1. Protocols

    1. Top of page
    2. Protocols
    3. Reviews
    4. Research Articles
    1. Biosynthesis of peptide fragments of eukaryotic GPCRs in Escherichia coli by directing expression into inclusion bodies (pages 213–218)

      Leah S. Cohen, Jeffrey M. Becker and Fred Naider

      Version of Record online: 1 APR 2010 | DOI: 10.1002/psc.1222

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      This review discusses a strategy for biosynthesis of fragments of integral membrane proteins. Production involves expression of a fusion protein, CNBr cleavage, and reverse phase HPLC purification. Specific examples are given for fragments of a G protein-coupled receptor; yields are 10– 20 mg per L of culture.

    2. On-resin conversion of Cys(Acm)-containing peptides to their corresponding Cys(Scm) congeners (pages 219–222)

      Daniel G. Mullen, Benjamin Weigel, George Barany and Mark D. Distefano

      Version of Record online: 1 APR 2010 | DOI: 10.1002/psc.1223

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      Standard Fmoc SPPS is performed to yield a fully protected, resin-bound peptide. Globally side chain protected peptide resin is treated with methoxycarbonylsulfenyl chloride in CH2Cl2 to effect Cys(Acm) to Cys(Scm) conversion. Treatment with Reagent K yields a deprotected peptide that retains Cys(Scm).

  2. Reviews

    1. Top of page
    2. Protocols
    3. Reviews
    4. Research Articles
    1. The depsipeptide method for solid-phase synthesis of difficult peptides (pages 223–230)

      Irene Coin

      Version of Record online: 12 APR 2010 | DOI: 10.1002/psc.1224

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      Peptides that are inaccessible due to the arising of aggregation phenomena may be more easily achieved via their depsipeptide analogs.

  3. Research Articles

    1. Top of page
    2. Protocols
    3. Reviews
    4. Research Articles
    1. Affinity of synthetic peptide fragments of MyoD for Id1 protein and their biological effects in several cancer cells (pages 231–241)

      Chiu-Heng Chen, Sheng-Chu Kuo, Li-Jiau Huang, Mei-Hua Hsu and Feng-Di T. Lung

      Version of Record online: 16 MAR 2010 | DOI: 10.1002/psc.1216

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      We designed and synthesized a series of peptide analogs of MyoD protein, and assayed for their in vitro bioactivities. Among the synthetic peptides, the peptide 3C (H-Tyr-Ile-Glu-Gly-Leu-Gln-Ala-Leu-Leu-Arg-Asp-Gln-NH2) exhibited high affinity for Id1 protein (KD = 12.5 µ M). It also exhibited anti-proliferative effects in cancer cells (IC50 = 25 µ M). Our results are promising for the development of antiproliferative agents and to our knowledge this is the first report that indicated the Id proteins' binding partners could be anticancer drug templets.

    2. Structure–activity relationship of a novel pentapeptide with cancer cell growth-inhibitory activity (pages 242–248)

      Masakatsu Kamiya, Keisuke Oyauchi, Yoshinori Sato, Takuya Yokoyama, Mofei Wang, Tomoyasu Aizawa, Yasuhiro Kumaki, Mineyuki Mizuguchi, Kunio Imai, Makoto Demura, Koichi Suzuki and Keiichi Kawano

      Version of Record online: 12 APR 2010 | DOI: 10.1002/psc.1225

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      Yamamarin, a pentapeptide with an amidated C-terminus (DILRG-NH2), significantly suppresses the proliferation of rat hepatoma (liver cancer) cells. We investigated the structure– activity relationship of yamamarin by in vitro assay and spectroscopic methods (CD and NMR) for various analogs. We revealed that the structure -RG-NH2 is essential for cell growth suppression.

    3. Study on structure and assembly of the third transmembrane domain of Slc11a1 (pages 249–255)

      Shuyan Xiao, Yuxia Wang, Lei Yang, Haiyan Qi, Chunyu Wang and Fei Li

      Version of Record online: 6 APR 2010 | DOI: 10.1002/psc.1230

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      The structure and self-assembly of the peptide corresponding to the third transmembrane domain of Slc11a1 and its E139A mutant are studied in HFIP aqueous solution by NMR and CD experiments. Both peptides form α-helical structure, but the E139A mutant is more hydrophobic and displays stronger tendency to aggregate.

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