Journal of Peptide Science

Cover image for Vol. 20 Issue 2

Special Issue: Chemical Protein Synthesis Meeting, April 3–6, 2013, Vienna

February 2014

Volume 20, Issue 2

Pages i–iii, 63–158

Issue edited by: Christian Becker

  1. Issue Information

    1. Top of page
    2. Issue Information
    3. Editorial
    4. Special Issue Reviews
    5. Protocols
    6. Special Issue Articles
    1. Issue information (pages i–iii)

      Article first published online: 20 JAN 2014 | DOI: 10.1002/psc.2557

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  2. Editorial

    1. Top of page
    2. Issue Information
    3. Editorial
    4. Special Issue Reviews
    5. Protocols
    6. Special Issue Articles
    1. You have free access to this content
      Chemical protein synthesis (page 63)

      Christian F.W. Becker, Ashraf Brik, Phil Dawson and Christian P. R. Hackenberger

      Article first published online: 20 JAN 2014 | DOI: 10.1002/psc.2607

  3. Special Issue Reviews

    1. Top of page
    2. Issue Information
    3. Editorial
    4. Special Issue Reviews
    5. Protocols
    6. Special Issue Articles
    1. Peptide ligation chemistry at selenol amino acids (pages 64–77)

      Lara R. Malins, Nicholas J. Mitchell and Richard J. Payne

      Article first published online: 28 NOV 2013 | DOI: 10.1002/psc.2581

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      This article provides a comprehensive review of ligation chemistry at selenol amino acids. Peptide ligation chemistry at selenocysteine is initially outlined as an effective means to generate selenocysteine-containing peptides by chemical synthesis or semisynthesis. The recent finding that selenocysteine residues can be chemoselectively deselenized to afford alanine residues following a ligation reaction has greatly expanded the utility of selenol ligation chemistry to access targets bearing internal, unprotected cysteine residues. This concept has recently been further exploited in ligation–chemoselective deselenization chemistry at proline and phenylalanine and is also discussed.

    2. Templated native chemical ligation: peptide chemistry beyond protein synthesis (pages 78–86)

      Olalla Vázquez and Oliver Seitz

      Article first published online: 7 JAN 2014 | DOI: 10.1002/psc.2602

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      Templated chemistry enables the design of reactions, which are under the control of third party molecules. This review describes native chemical ligation reactions that are explored as tools in nucleic acid diagnosis, origin-of-life studies and gene-expression-specific therapies.

  4. Protocols

    1. Top of page
    2. Issue Information
    3. Editorial
    4. Special Issue Reviews
    5. Protocols
    6. Special Issue Articles
    1. Synthesis of thioester peptides for the incorporation of thioamides into proteins by native chemical ligation (pages 87–91)

      Solongo Batjargal, Yun Huang, Yanxin J. Wang and E. James Petersson

      Article first published online: 9 JAN 2014 | DOI: 10.1002/psc.2589

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      Thioamides can be used as photoswitches, as reporters of local environment, as inhibitors of enzymes, and as fluorescence quenchers. We have recently demonstrated the incorporation of thioamides into polypeptides and proteins using native chemical ligation (NCL). In this protocol, we describe procedures for the synthesis of a thioamide precursor and an NCL-ready thioamide-containing peptide using Dawson's N-acyl-benzimidazolinone (Nbz) process. We include a description of the synthesis by NCL of a thioamide-labeled fragment of the neuronal protein α-synuclein.

    2. Tidbits for the synthesis of bis(2-sulfanylethyl)amido (SEA) polystyrene resin, SEA peptides and peptide thioesters (pages 92–97)

      Nathalie Ollivier, Laurent Raibaut, Annick Blanpain, Rémi Desmet, Julien Dheur, Reda Mhidia, Emmanuelle Boll, Hervé Drobecq, Silvain L. Pira and Oleg Melnyk

      Article first published online: 19 NOV 2013 | DOI: 10.1002/psc.2580

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      A detailed protocol for the preparation of bis(2-sulfanylethyl)amino polystyrene resin as a starting point for the synthesis of C-terminal bis(2-sulfanylethyl)amido peptides and of peptide thioesters derived from 3-mercaptopropionic acid is described.

    3. Safe and efficient Boc-SPPS for the synthesis of glycopeptide-α-thioesters (pages 98–101)

      Masayuki Izumi, Masumi Murakami, Ryo Okamoto and Yasuhiro Kajihara

      Article first published online: 6 JAN 2014 | DOI: 10.1002/psc.2608

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      The glycopeptide-thioesters are the key components for chemical synthesis of glycoproteins. We report a general procedure for the preparation of glycopeptide-thioesters employing a safe and efficient Boc-solid phase peptide synthesis using 10% sulfuric acid/dioxane for Boc deprotection, low-acidity TfOH conditions for global deprotection, and thiolysis for release of the thioester from the resin.

  5. Special Issue Articles

    1. Top of page
    2. Issue Information
    3. Editorial
    4. Special Issue Reviews
    5. Protocols
    6. Special Issue Articles
    1. New semi-synthesis of ubiquitin C-terminal conjugate with 7-amino-4-methylcoumarin (pages 102–107)

      Yi-Tong Li, Jun Liang, Jia-Bin Li, Ge-Min Fang, Yong Huang and Lei Liu

      Article first published online: 3 OCT 2013 | DOI: 10.1002/psc.2568

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      Native chemical ligation of a recombinant peptide hydrazide with a Gly-peptide carrying a removal auxiliary was examined and used to synthesize ubiquitin C-terminal conjugates.

    2. Dynamic covalent side-chain cross-links via intermolecular oxime or hydrazone formation from bifunctional peptides and simple organic linkers (pages 108–114)

      Conor M. Haney and W. Seth Horne

      Article first published online: 9 JAN 2014 | DOI: 10.1002/psc.2596

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      We report a method for the synthesis of side-chain to side-chain cyclic peptides based on the intermolecular reaction between a linear peptide with two aminooxy or hydrazide side chains and an organic dialdehyde linker. The dynamic covalent nature of the Schiff bases in the cyclic products enables the creation of mixtures where product composition changes in response to experimental conditions.

    3. Generation of an intramolecular three-color fluorescence resonance energy transfer probe by site-specific protein labeling (pages 115–120)

      Stephanie Voss, Lei Zhao, Xi Chen, Frank Gerhard and Yao-Wen Wu

      Article first published online: 6 JAN 2014 | DOI: 10.1002/psc.2590

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      We describe a method for site-specific labeling of a given protein with three distinct fluorophores. This strategy facilitates triple FRET analysis on proteins.

    4. SUMOylated RanGAP1 prepared by click chemistry (pages 121–127)

      Nadine D. van Treel and Henning D. Mootz

      Article first published online: 15 DEC 2013 | DOI: 10.1002/psc.2591

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      A chemical SUMO1-RanGAP1 conjugate was generated via the copper-catalyzed alkyne-azide cycloaddition (CuAAC). The triazole-linked analog was compared to the native isopeptide-linked conjugate and showed similar binding to form the multiprotein complex with RanBP2 and Ubc9. Our study illustrates advantages and disadvantages of two different routes for SUMO conjugation by CuAAC and further underlines the potential of chemical conjugates to investigate the biochemistry of ubiquitin and ubiquitin-like post-translational modifiers.

    5. Engineering the oxyanion hole of trypsin for promoting the reverse of proteolysis (pages 128–136)

      Lars Franke, Sandra Liebscher and Frank Bordusa

      Article first published online: 20 DEC 2013 | DOI: 10.1002/psc.2597

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      For optimizing trypsin for peptide and protein synthesis, the oxyanion hole of the enzyme was engineered by rational mutagenesis. From the six mutated trypsin variants, two enzyme hits with an artificial proline mutation either in position 192 or in position 194 could be identified. Model reactions qualify both biocatalysts as efficient coupling enzymes not only for peptide but also for protein semisynthesis.

    6. Total chemical synthesis of a membrane protein domain analogue containing two transmembrane helices: functional reconstitution of the semisynthetic sensory rhodopsin/transducer complex (pages 137–144)

      Marc Dittmann, Ralf Seidel, Igor Chizhov and Martin Engelhard

      Article first published online: 6 JAN 2014 | DOI: 10.1002/psc.2605

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      We developed a protocol for the synthesis of a membrane protein domain analogue containing two transmembrane helices. The product was refolded into micelles and showed functional properties as determined by binding studies to its cognate receptor NpSRII and by photocycle experiments. This work demonstrates that membrane proteins can be successfully synthesized by chemical means paving the way for tailor-made modifications.

    7. Chemo-enzymatic three-fragment assembly of semisynthetic proteins (pages 145–151)

      Lena Schmohl and Dirk Schwarzer

      Article first published online: 9 JAN 2014 | DOI: 10.1002/psc.2600

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      Sortase-mediated ligation in combination with site-specific bioconjugation catalyzed by the 4′-phosphopantetheine transferase Sfp was used for the orthogonal assembly of semisynthetic proteins from three fragments in a one-pot reaction. The assembled proteins are linked at the N-terminal junction with a 4′-phosphopantetheine moiety and with a peptide bond at the C-terminal ligation site. This method was established for model proteins derived from fluorescence resonance energy transfer reporters.

    8. A sequence-function analysis of the silica precipitating silaffin R5 peptide (pages 152–158)

      Carolin C. Lechner and Christian F. W. Becker

      Article first published online: 5 NOV 2013 | DOI: 10.1002/psc.2577

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      A functional analysis of the R5 peptide highlights the characteristics of its amino acid sequence essential for silica precipitating activity. The RRIL amino acids are important for peptide self-assembly and lysine residues mediate silica formation. Overall, the well-balanced arrangement of charges and functionalities in the amino acid sequence of R5 turns out to be perfectly evolved for efficient silica precipitation.

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