Chemistry and Biochemistry of Glycosylation

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Carbohydrates".

Deadline for manuscript submissions: closed (31 October 2023) | Viewed by 2091

Special Issue Editors


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Guest Editor
University Center for Bioscience and Biotechnology, Department of Medical Laboratory Science and Biotechnology, National Cheng Kung University, Tainan, Taiwan
Interests: glycobiology; glycosylation

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Guest Editor
Instrumentation Center, National Taiwan University, Taipei, Taiwan
Interests: mass spectrometry; glycobiology

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Guest Editor
Department of Bioscience and Biotechnology, National Taiwan Ocean University, Keelung, Taiwan
Interests: organic chemistry; mass spectrometry

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Guest Editor
Medical Laboratory, Medical Education and Research Center, Kaohsiung Armed Forces General Hospital, Kaohsiung, Taiwan
Interests: glycobiology; cancer biology; carcinogenesis; environmental toxicology
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Special Issue Information

Dear Colleagues,

Glycosylation plays a crucial role in the co- and post-translational modifications of more than 90% of proteins in eukaryotic cells. Glycans expressed on cell surface participate in many important cellular events by interacting with their corresponding proteins or receptors. Alterations in carbohydrate compositions are known to correlate with the changes in protein stability and clearance, as well as various important biological functions including cell-cell adhesion, inflammation, infection of bacteria and viruses, tumorigenesis, and metastasis. Transformation of malignancy is frequently accompanied by an intense alteration in the structures of oligosaccharides on proteins of cell surface. The molecular changes that occur upon malignant transformation can be characterized using specific monoclonal antibodies and mass spectrometry. The changes in glycosylation include both the under- and overexpression of naturally occurring glycans, as well as neo-expression of glycans normally restricted to embryonic tissues.  Hence, this special issue aims to collect research papers or reviews that can improve our knowledge on chemistry and biochemistry of glycobiology, as well as functional glycomics. You are welcome to submit your current research work.

Dr. Chuan-Fa Chang
Dr. Hsin-Yi Wu
Dr. Pang-Hung Hsu
Dr. Yung-Kuo Lee
Guest Editors

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Keywords

  • glycobiology
  • chemistry
  • biochemistry

Published Papers (1 paper)

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Research

19 pages, 3308 KiB  
Article
Enzymatic Glyco-Modification of Synthetic Membrane Systems
by Dylan Jabeguero, Lina Siukstaite, Chunyue Wang, Anna Mitrovic, Serge Pérez, Olga Makshakova, Ralf P. Richter, Winfried Römer and Christelle Breton
Biomolecules 2023, 13(2), 335; https://doi.org/10.3390/biom13020335 - 9 Feb 2023
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Abstract
The present report assesses the capability of a soluble glycosyltransferase to modify glycolipids organized in two synthetic membrane systems that are attractive models to mimic cell membranes: giant unilamellar vesicles (GUVs) and supported lipid bilayers (SLBs). The objective was to synthesize the Gb3 [...] Read more.
The present report assesses the capability of a soluble glycosyltransferase to modify glycolipids organized in two synthetic membrane systems that are attractive models to mimic cell membranes: giant unilamellar vesicles (GUVs) and supported lipid bilayers (SLBs). The objective was to synthesize the Gb3 antigen (Galα1,4Galβ1,4Glcβ-Cer), a cancer biomarker, at the surface of these membrane models. A soluble form of LgtC that adds a galactose residue from UDP-Gal to lactose-containing acceptors was selected. Although less efficient than with lactose, the ability of LgtC to utilize lactosyl–ceramide as an acceptor was demonstrated on GUVs and SLBs. The reaction was monitored using the B-subunit of Shiga toxin as Gb3-binding lectin. Quartz crystal microbalance with dissipation analysis showed that transient binding of LgtC at the membrane surface was sufficient for a productive conversion of LacCer to Gb3. Molecular dynamics simulations provided structural elements to help rationalize experimental data. Full article
(This article belongs to the Special Issue Chemistry and Biochemistry of Glycosylation)
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