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Molecules
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Chemoselective Ligations
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Chemoselective Ligations

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (30 June 2018) | Viewed by 10529

Special Issue Editors

Prof. Dr. Olivier Renaudet

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Guest Editor
Department of Molecular Chemistry, University Grenoble-Alpes, Saint-Martin-d'Hères, France
Interests: carbohydrates; peptides; multivalency; chemical ligations; glycoconjugates; synthetic vaccines; antiadhesive agents; lectins; microarrays
Dr. Nicolas Spinelli

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Guest Editor
Department of Molecular Chemistry, University Grenoble-Alpes, Grenoble, France
Interests: oligonucleotide; oxime; CuAAC; peptides; aptamers; G-quadruplexes; biosensors

Special Issue Information

Dear Colleagues,

Chemoselective ligations are undoubtedly the methods of choice for the synthesis of well-defined and complex biomacromolecular systems, based on peptides, carbohydrates, and/or oligonucleotides. This Special Issue will be dedicated to recent advances in this field, and will also have a special focus on biological applications of the resulting structures.

Olivier Renaudet
Nicolas Spinelli
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • carbohydrates
  • peptides
  • oligonucleotides
  • supramolecular chemistry
  • chemical ligation
  • bioorthogonality
  • click-chemistry

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Published Papers (2 papers)

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Research

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15 pages, 17160 KiB  
Article
Immobilization of Staphylococcus aureus Sortase A on Chitosan Particles and Its Applications in Peptide-to-Peptide Ligation and Peptide Cyclization
by Min Yang, Haofei Hong, Shaozhong Liu, Xinrui Zhao and Zhimeng Wu
Molecules 2018, 23(1), 192; https://doi.org/10.3390/molecules23010192 - 19 Jan 2018
Cited by 4 | Viewed by 4937
Abstract
Chitosan macro-particles prepared by the neutralization method were applied to Sortase A (SrtA) immobilization using glutaraldehyde as a crosslinking agent. The particles were characterized by Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). Response surface methodology (RSM) was employed to optimize [...] Read more.
Chitosan macro-particles prepared by the neutralization method were applied to Sortase A (SrtA) immobilization using glutaraldehyde as a crosslinking agent. The particles were characterized by Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). Response surface methodology (RSM) was employed to optimize the immobilization process. An average specific activity of 3142 U (mg protein)−1 was obtained under optimized immobilization conditions (chitosan concentration 3%, SrtA concentration 0.5 mg·mL−1, glutaraldehyde concentration 0.5%, crosslinking and immobilization at 20 °C, crosslinking for 3 h, and an immobilization time of 8 h). The transpeptidase activity of immobilized SrtA was proved by a peptide-to-peptide ligation with a conversion yield approximately at 80%, and the immobilized catalyst was successfully reused for five cycles without obvious activity loss. Moreover, the scale-up capability of using immobilized SrtA to catalyze a head-to-tail peptide cyclization was investigated in a batch reaction and the conversion yield was more than 95% when using 20 mg of peptide as a substrate. Full article
(This article belongs to the Special Issue Chemoselective Ligations)
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Review

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14 pages, 1691 KiB  
Review
Chemical Reporters and Their Bioorthogonal Reactions for Labeling Protein O-GlcNAcylation
by Eun Ju Kim
Molecules 2018, 23(10), 2411; https://doi.org/10.3390/molecules23102411 - 20 Sep 2018
Cited by 11 | Viewed by 5218
Abstract
Protein O-GlcNAcylation is a non-canonical glycosylation of nuclear, mitochondrial, and cytoplasmic proteins with the attachment of a single O-linked β-N-acetyl-glucosamine (O-GlcNAc) moiety. Advances in labeling and identifying O-GlcNAcylated proteins have helped improve the understanding of O [...] Read more.
Protein O-GlcNAcylation is a non-canonical glycosylation of nuclear, mitochondrial, and cytoplasmic proteins with the attachment of a single O-linked β-N-acetyl-glucosamine (O-GlcNAc) moiety. Advances in labeling and identifying O-GlcNAcylated proteins have helped improve the understanding of O-GlcNAcylation at levels that range from basic molecular biology to cell signaling and gene regulation to physiology and disease. This review describes these advances in chemistry involving chemical reporters and their bioorthogonal reactions utilized for detection and construction of O-GlcNAc proteomes in a molecular mechanistic view. This detailed view will help better understand the principles of the chemistries utilized for biology discovery and promote continued efforts in developing new molecular tools and new strategies to further explore protein O-GlcNAcylation. Full article
(This article belongs to the Special Issue Chemoselective Ligations)
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