Journal of Peptide Science

Cover image for Vol. 16 Issue 12

December 2010

Volume 16, Issue 12

Pages 675–722

  1. Protocol

    1. Top of page
    2. Protocol
    3. Research Articles
    1. ChemMatrix® for complex peptides and combinatorial chemistry (pages 675–678)

      Yésica García-Ramos, Marta Paradís-Bas, Judit Tulla-Puche and Fernando Albericio

      Article first published online: 16 SEP 2010 | DOI: 10.1002/psc.1282

      Thumbnail image of graphical abstract

      CM resin is a totally PEG-based resin, made exclusively from primary ether bonds and therefore highly chemically stable. It exhibits good loadings and is user friendly because of its free-flowing form upon drying. It has shown an excellent performance for the preparation of hydrophobic, highly structured poly-Arg peptides, and small proteins in combination with ψ Pros. Like other PEG-based resins, CM resin swells well in biocompatible solvents such as water, extending its applications in the field of combinatorial chemistry.

  2. Research Articles

    1. Top of page
    2. Protocol
    3. Research Articles
    1. Monitoring the allyl ester deprotection by HR MAS NMR in BAL-solid phase peptide synthesis (pages 679–686)

      T. Duchène, C. Mihai, R. Willem and D. Tourwé

      Article first published online: 5 SEP 2010 | DOI: 10.1002/psc.1278

      Thumbnail image of graphical abstract

      The backbone amide linker strategy, in which the growing peptide chain is anchored to a solid support via a backbone amide nitrogen, has proven to be successful for the synthesis of cyclic peptides. Optimization of the reaction conditions for the synthesis of c(Gly-Trp-bAla-Phe) could be accomplished by the help of HR MAS NMR. Signal vanishing of HR MAS NMR resonances were encountered and proven to be originated from interchain aggregations of peptide chains.

    2. Influence of charge distribution on the discrepant MS/MS fragmentation of the native and oxidized FMRF: evidence for the mobile proton model (pages 687–692)

      Wansong Zong, Rutao Liu, Feng Sun, Pengjun Zhang and Qifei Xu

      Article first published online: 16 SEP 2010 | DOI: 10.1002/psc.1286

      Thumbnail image of graphical abstract

      Side-chain oxidation on FMRF produces the oxidation products FM(O)RF and FM(O2)RF. With the increase of oxidation extent of FMRF, more negative charge was deposited in the main protonation sites of the oxidation products, resulting in the highly protonated amide bonds and the easily fragmented amide bonds.

    3. Analysis of peptides and proteins in their binding to GroEL (pages 693–700)

      Yali Li, Zhida Zheng, Andrew Ramsey and Lingling Chen

      Article first published online: 1 SEP 2010 | DOI: 10.1002/psc.1288

      Thumbnail image of graphical abstract

      Small peptides are useful to reveal structural basis for GroEL-substrate protein interaction. This study compares various aspects of a peptide termed SBP with those of GroEL substrate proteins in their binding to GroEL. We found that peptides like SBP may represent many features of substrate proteins in their interaction with GroEL, but they can not mimic the binding cooperativity due to the lack of a contiguous linker that connects all the GroEL-bound peptides.

    4. Nanopore analysis of tethered peptides (pages 701–708)

      Howard Meng, Dielle Detillieux, Christian Baran, Besnik Krasniqi, Christopher Christensen, Claudia Madampage, Radu I. Stefureac and Jeremy S. Lee

      Article first published online: 2 SEP 2010 | DOI: 10.1002/psc.1289

      Thumbnail image of graphical abstract

      Threading the needle. Up to four short peptides were attached to a single benzene ring to produce peptide bundles and their ability to thread through the α-hemolysin pore was assessed. Bundles of one or two strands readily translocated, whereas three- and four-stranded bundles produced many bumping and intercalation events as well as permanent blockages. The results suggest that proteins must completely unfold in order to thread through the pore.

    5. Synthesis and conformational analysis of salivary proline-rich peptide P-B (pages 709–715)

      Elżbieta Kamysz and Emilia Sikorska

      Article first published online: 19 SEP 2010 | DOI: 10.1002/psc.1297

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      The present work describes the synthesis and conformational studies of salivary proline-rich peptide P[BOND]B. The circular dichroism spectroscopy, Fourier-transform infrared spectroscopy and molecular modeling methods have been used for conformational studies of P–B.

    6. Synthesis and analysis of the membrane proximal external region epitopes of HIV-1 (pages 716–722)

      Sampat Ingale, Johannes S. Gach, Michael B. Zwick and Philip E. Dawson

      Article first published online: 23 NOV 2010 | DOI: 10.1002/psc.1325

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      The primary interacting residues for 4E10 binding are WF; new analogs containing unnatural amino acids have been synthesized compatible with 4E10 binding in this region. Backbone modifications with Aib and Api at C-terminal tail of the epitope yielded better mimics of the MPER that will more likely elicit neutralizing antibodies.

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