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Special Issue "Protein Conjugates and Bioconjugate Chemistry"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry, Molecular Biology and Biophysics".

Deadline for manuscript submissions: closed (29 February 2012)

Special Issue Editor

Guest Editor
Prof. Dr. Teruyuki Nagamune

Department of Bioengineering, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan
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Special Issue Information

Dear Colleagues,

The modification or conjugation of proteins, DNAs, and other biopolymers with functional molecules has become a very powerful research tool in biological science, biomedical research, and biotechnology. In particular, in the current post genomic era, much research requires chemically modified proteins or protein-bioconjugates that are impossible to prepare by standard ribosomal synthesis. In addition to the applications to research tools, there are a growing number of commercial applications of these modified biomolecules, including DNA sequencing, gene SNP analysis, clinical immunoassays, PEGylation of pharmaceutical proteins and so on.

Various techniques to precisely (site specifically) modify proteins with diverse natural and unnatural functionalities have been developed in the last two decades. These methods range from classical bioconjugation reactions to more sophisticated approaches such as the biomimetic transamination reaction, affinity-based protein surface labeling, peptide-/protein-tag fusions, and nonsense suppression mutagenesis.  Protein ligation is another powerful protein engineering technique, which allows fully unprotected synthetic and recombinant polypeptides to be regioselectively joined together to build up a target protein molecule. To date, several chemical and enzymatic peptide ligation methods have been reported.

This volume invites original contributions on all aspects of conjugation chemistry and biochemistry, including the preparation, characterization, and chemical and biological properties of molecular conjugates such as antibodies, nucleic acids, lipids, carbohydrates, or other biologically active molecules with any molecular groups that add useful properties (fluorophores, enzymes, drugs, toxins, ligands, etc.). The critical reviews covering both fundamental and applied aspects of this exciting field are also welcome.

Prof. Dr. Teruyuki Nagamune
Guest Editor

Keywords

  • biomolecular conjugates
  • bioconjugation chemistry
  • chemical ligation
  • protein ligation
  • site-specific chemical and enzymatic modification
  • PEGylation

Published Papers (2 papers)

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Research

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Open AccessArticle Characterization and Comparison of Fumonisin B1-Protein Conjugates by Six Methods
Int. J. Mol. Sci. 2012, 13(1), 84-96; doi:10.3390/ijms13010084
Received: 10 October 2011 / Revised: 8 November 2011 / Accepted: 28 November 2011 / Published: 22 December 2011
Cited by 7 | PDF Full-text (185 KB) | HTML Full-text | XML Full-text
Abstract
In order to generate an antibody against a small hapten molecule, the hapten is cross-linked with carrier protein to make it immunogenic. In this study, the hapten (Fumonisin B1, FB1) was coupled to ovalbumin (OVA) and bovine serum albumin
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In order to generate an antibody against a small hapten molecule, the hapten is cross-linked with carrier protein to make it immunogenic. In this study, the hapten (Fumonisin B1, FB1) was coupled to ovalbumin (OVA) and bovine serum albumin (BSA), respectively by a short cross-linker reagent (glutaraldehyde, GA). To develop a technique for detecting the conjugation, the hapten-protein conjugates (FB1-OVA and FB1-BSA) were characterized thoroughly by ultraviolet (UV) spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS), respectively. The molecular weights of FB1-BSA and FB1-OVA were 74,355.301 Da and 48,009.212 Da, respectively determined by the method of MALDI-TOF-MS. The molecular coupling ratios were 11 and 5 in FB1-BSA and FB1-OVA, respectively. In this experiment, MALDI-TOF-MS was selected as the most efficient method to evaluate the cross-linking effect and calculate the molecular coupling ratio. Full article
(This article belongs to the Special Issue Protein Conjugates and Bioconjugate Chemistry)

Review

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Open AccessReview Design and Synthesis of Binding Growth Factors
Int. J. Mol. Sci. 2012, 13(5), 6053-6072; doi:10.3390/ijms13056053
Received: 5 March 2012 / Revised: 10 April 2012 / Accepted: 9 May 2012 / Published: 18 May 2012
Cited by 15 | PDF Full-text (670 KB) | HTML Full-text | XML Full-text
Abstract
Growth factors play important roles in tissue regeneration. However, because of their instability and diffusible nature, improvements in their performance would be desirable for therapeutic applications. Conferring binding affinities would be one way to improve their applicability. Here we review techniques for conjugating
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Growth factors play important roles in tissue regeneration. However, because of their instability and diffusible nature, improvements in their performance would be desirable for therapeutic applications. Conferring binding affinities would be one way to improve their applicability. Here we review techniques for conjugating growth factors to polypeptides with particular affinities. Conjugation has been designed at the level of gene fusion and of polypeptide ligation. We summarize and discuss the designs and applications of binding growth factors prepared by such conjugation approaches. Full article
(This article belongs to the Special Issue Protein Conjugates and Bioconjugate Chemistry)

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