Journal of Peptide Science

Cover image for Journal of Peptide Science

March 2010

Volume 16, Issue 3

Pages 123–164

  1. Rapid Communications

    1. Top of page
    2. Rapid Communications
    3. Research Articles
    1. An improved procedure for the synthesis of dehydroamino acids and dehydropeptides from the carbonate derivatives of serine and threonine using tetrabutylammonium fluoride (pages 123–125)

      Ramesh Ramapanicker, Roli Mishra and Srinivasan Chandrasekaran

      Version of Record online: 28 JAN 2010 | DOI: 10.1002/psc.1210

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      An efficient procedure for the synthesis of dehydroamino acids and dehydropeptides from hydroxy amino acids.

  2. Research Articles

    1. Top of page
    2. Rapid Communications
    3. Research Articles
    1. Conformational properties of the residues connected by ester and methylated amide bonds: theoretical and solid state conformational studies (pages 126–135)

      Dawid Siodłak and Anna Janicki

      Version of Record online: 28 JAN 2010 | DOI: 10.1002/psc.1208

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      The ester bond in the peptide main chain has a different influence on the residues following and preceding in the sequence. Furthermore, the residues which have both ester and methylated amide bonds have different conformational properties and the location of these modifications (N-terminus or C-terminus) is also important. The neighbouring ester linkage does not increase the tendency towards the configuration cis of the amide bond.

    2. A convenient microwave-enhanced solid-phase synthesis of short chain N-methyl-rich peptides (pages 136–140)

      Hortensia Rodríguez, Margarita Suarez and Fernando Albericio

      Version of Record online: 2 FEB 2010 | DOI: 10.1002/psc.1209

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      N-Methyl-rich peptides are rapidly and efficiently prepared by a microwave-assisted Fmoc/tBu solid-phase method

    3. Selective cleavage of an azaGly peptide bond by copper(II). Long-range effect of histidine residue (pages 141–147)

      Reda Mhidia and Oleg Melnyk

      Version of Record online: 3 FEB 2010 | DOI: 10.1002/psc.1211

      Thumbnail image of graphical abstract

      Cu(II), unlike other metal ions such as Fe(II), Fe(III), Pd(II) or Pt(II), induces the cleavage of azaGly peptides at room temperature and pH 7.3. The presence of an His residue downstream or upstream from azaGly moiety accelerated the cleavage reaction. The influence of His residue on the cleavage rate was minimal when His and Agly were adjacent, whereas large effects were observed for distant His residues.

    4. The oxidative products of methionine as site and content biomarkers for peptide oxidation (pages 148–152)

      Wansong Zong, Rutao Liu, Meijie Wang, Pengjun Zhang, Feng Sun and Yanmin Tian

      Version of Record online: 9 FEB 2010 | DOI: 10.1002/psc.1212

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      In the three model peptides of DRVYVHPF, FMRF and RPPGFSPYR, the Met containing peptide FMRF was prone to undergo UV/H2O2 oxidization in time dependency, forming the sulfoxide derivative FM(O)RF. Correspondingly, methionine sulfoxide in peptides and proteins may well represent good biomarkers for oxidative stress.

    5. Controlling the helical screw sense of peptides with C-terminal L-valine (pages 153–158)

      Yosuke Demizu, Nanako Yamagata, Yukiko Sato, Mitsunobu Doi, Masakazu Tanaka, Haruhiro Okuda and Masaaki Kurihara

      Version of Record online: 2 FEB 2010 | DOI: 10.1002/psc.1213

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      The present study describes the insertion of a chiral amino acid (L-Val) at the C-terminus is able to control the screw sense of helical peptides that do not exhibit a screw sense bias in solution and/or the solid state.

    6. Identification of small peptides mimicking the R2 C-terminus of Mycobacterium tuberculosis ribonucleotide reductase (pages 159–164)

      Daniel J. Ericsson, Johanna Nurbo, Daniel Muthas, Kalle Hertzberg, Gunnar Lindeberg, Anders Karlén and Torsten Unge

      Version of Record online: 2 FEB 2010 | DOI: 10.1002/psc.1214

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      Mycobacterium tuberculosis ribonucleotide reductase is inhibited by disrupting the formation of the holoenzyme. Here, synthesis and binding affinity, evaluated by competitive fluorescence polarization, is described for small, N-protected peptides and amino acids.

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