Journal of Peptide Science

Cover image for Vol. 17 Issue 6

June 2011

Volume 17, Issue 6

Pages 413–486

  1. Reviews

    1. Top of page
    2. Reviews
    3. Research Articles
    1. Triplet–triplet energy transfer studies on conformational dynamics in peptides and a protein (pages 413–419)

      Andreas Reiner

      Version of Record online: 24 FEB 2011 | DOI: 10.1002/psc.1353

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      TTET allows to measure contact formation between two amino acid side chains on the picosecond to microsecond time scale. This review summarizes studies on the chain dynamics of unstructured peptides, as well as TTET experiments to probe conformational dynamics in α-helical peptides and in a small protein.

  2. Research Articles

    1. Top of page
    2. Reviews
    3. Research Articles
    1. Effect of one D-Leu residue on right-handed helical -L-Leu-Aib- peptides in the crystal state (pages 420–426)

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

      Version of Record online: 21 FEB 2011 | DOI: 10.1002/psc.1332

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      Four diastereomeric -Leu-Leu-Aib-Leu-Leu-Aib- peptides were synthesized, and the conformations of their peptides were studied in the crystalline state.

    2. Cyclic neoglycodecapeptides: how to increase their inhibitory activity and selectivity on lectin/toxin binding to a glycoprotein and cells (pages 427–437)

      Sabine André, Olivier Renaudet, Isabelle Bossu, Pascal Dumy and Hans-Joachim Gabius

      Version of Record online: 4 FEB 2011 | DOI: 10.1002/psc.1338

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      As blocking distinct glycan–lectin interactions is becoming a therapeutic aim, the capacity of cyclic neoglycodecapeptides to serve as scaffold for bioactive carbohydrate ligands was tested. Using assay systems of increasing biorelevance and medically relevant lectins evidence for suitability and target selectivity among related proteins is presented, these glycoclusters e.g. potently blocking cell surface binding of a human galectin as shown.

    3. Immunomodulatory efficacy of nisin—a bacterial lantibiotic peptide (pages 438–444)

      D. Begde, S. Bundale, P. Mashitha, J. Rudra, N. Nashikkar and A. Upadhyay

      Version of Record online: 4 FEB 2011 | DOI: 10.1002/psc.1341

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      Both human neutrophils and lymphocytes seem to undergo cell death without substantial DNA fragmentation when treated with the lantibiotic nisin in vitro. In fact, nisin induced formation of NETs in isolated human neutrophils. Nisin thus demonstrated its potential as an effective in vitro immunomodulatory agent.

    4. Derivatization of peptides as quaternary ammonium salts for sensitive detection by ESI-MS (pages 445–453)

      Marzena Cydzik, Magdalena Rudowska, Piotr Stefanowicz and Zbigniew Szewczuk

      Version of Record online: 24 FEB 2011 | DOI: 10.1002/psc.1342

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      A series of model peptides in the form of N-terminal quaternary ammonium salts were efficiently prepared by the solid phase synthesis. Tandem mass spectrometric analysis of the peptide quaternary ammonium derivatives was shown to provide sequence confirmation and enhanced detection. This strategy offers also a significant increase in ionization efficiency, allowing the detection of femtomolar amounts of peptides, which could be useful in analysis of the one-bead-one-compound combinatorial peptide libraries prepared by the split-and-mix method.

    5. Structure–activity relationship study of antioxidative peptides by QSAR modeling: the amino acid next to C-terminus affects the activity (pages 454–462)

      Yao-Wang Li, Bo Li, Jiguo He and Ping Qian

      Version of Record online: 13 APR 2011 | DOI: 10.1002/psc.1345

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      Quantitative structure-activity relationship (QSAR) modeling was performed respectively on synthetic tripeptides and tetrapeptides for understanding the structural characteristics of antioxidative peptides. According to the QSAR modeling, hydrogen bond property of the amino acid residue next to C-terminus and the hydrophobicity of N-terminus are significant for antioxidant activity, meanwhile electronic properties of C-terminus also affects the activity.

    6. Chemical synthesis and evaluation of a backbone-cyclized minimized 2-helix Z-domain (pages 463–469)

      Peter Järver, Cecilia Mikaelsson and Amelie Eriksson Karlström

      Version of Record online: 24 FEB 2011 | DOI: 10.1002/psc.1346

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      The article presents the synthesis and characterization of a backbone-cyclized two-helix Z-domain denoted Zmin. The molecule resists heating to 90 °C, has retained high affinity to IgG and can be used for affinity capture of IgG. Moreover, the data presented indicate that the cyclic peptide could be useful for other applications and serve as a minimal scaffold for the introduction of other binding characteristics.

    7. Low-generation asymmetric dendrimers exhibit minimal toxicity and effectively complex DNA (pages 470–478)

      Neha Shah, Raymond J. Steptoe and Harendra S. Parekh

      Version of Record online: 24 FEB 2011 | DOI: 10.1002/psc.1347

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      In this study, we investigated the physico-chemical characteristics of low-generation asymmetric peptide dendrimers and their ability to complex pDNA under various conditions. We compared the morphology of our dendriplexes with a commercially available dendrimer and also assessed their cytotoxicity profile. We report that the asymmetric dendrimers form toroids upon complexing with DNA, and that this is dependent upon ionic strength of the complexing solution. Our dendriplexes are also minimally toxic even when very high N:P ratios are employed.

    8. Amino acid sequence preferences to control cell-specific organization of endothelial cells, smooth muscle cells, and fibroblasts (pages 479–486)

      Kei Kanie, Ryuji Kato, Yingzi Zhao, Yuji Narita, Mina Okochi and Hiroyuki Honda

      Version of Record online: 24 FEB 2011 | DOI: 10.1002/psc.1355

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      Cell-specific preference on single amino acid peptides were investigated on peptide array. The cell adhesion and proliferation of endothelial cells (ECs), smooth muscle cells (SMCs), and fibroblast (FBs) were compared in the scope of future application to cardiovascular medical implants. ECs and FBs adhesion were controlled by hydrophobic residues, and SMCs proliferation was controlled by aromatic residues for proliferation. Our result suggests that domain-like physicochemical properties are more important for cell preference than exact residue.