Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
7.8
5.6
Journals
IJMS
Special Issues
New Advances in Glycobiotechnology
ijms-logo
Submit to IJMS Review for IJMS Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

New Advances in Glycobiotechnology

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

Deadline for manuscript submissions: closed (15 March 2024) | Viewed by 1906

Special Issue Editor

Prof. Dr. Hiroshi Hinou

E-Mail Website
Guest Editor
Laboratory of Advanced Chemical Biology, Hokkaido University, Sapporo 001-0021, Japan
Interests: organic chemistry; glycotechnology; glycomedicine; chemical biology; inhibitor; synthetic probe; mass spectrometry; microarray; infection; immunity; cancer; lectin; glycotyping

Special Issue Information

Dear Colleagues, 

Glycans (carbohydrates) are the fundamental substance in life, starting from photosynthesis. As a result, all living organisms (cells, tissues, etc.) are covered with glycocalyx, and these glycocalyces’ physical and biochemical functions have contributed to the adaptation (evolution) and diversity of organisms. In particular, biosynthetic pathways, sites of utilization, and forms of utilization are impossible to capture solely by deciphering the genes of single organisms. For this reason, the development of technologies to understand and utilize glycan functions has been vigorously conducted from various approaches. This Special Issue focuses on the development of glycobiotechnology, and calls for original research papers and review articles. Any technology and means (analytical, synthetic, or utilization methods) can be used as long as they are related to this subject.

We look forward to your active contributions.

Prof. Dr. Hiroshi Hinou
Guest Editor

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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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.

Published Papers (2 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

15 pages, 3128 KiB  
Article
Galf-Specific Neolectins: Towards Promising Diagnostic Tools
by Mateja Seničar, Benoît Roubinet, Pierre Lafite, Laurent Legentil, Vincent Ferrières, Ludovic Landemarre and Richard Daniellou
Int. J. Mol. Sci. 2024, 25(9), 4826; https://doi.org/10.3390/ijms25094826 - 28 Apr 2024
Viewed by 599
Abstract
In the absence of naturally available galactofuranose-specific lectin, we report herein the bioengineering of GalfNeoLect, from the first cloned wild-type galactofuranosidase (Streptomyces sp. strain JHA19), which recognises and binds a single monosaccharide that is only related to nonmammalian species, usually [...] Read more.
In the absence of naturally available galactofuranose-specific lectin, we report herein the bioengineering of GalfNeoLect, from the first cloned wild-type galactofuranosidase (Streptomyces sp. strain JHA19), which recognises and binds a single monosaccharide that is only related to nonmammalian species, usually pathogenic microorganisms. We kinetically characterised the GalfNeoLect to confirm attenuation of hydrolytic activity and used competitive inhibition assay, with close structural analogues of Galf, to show that it conserved interaction with its original substrate. We synthetised the bovine serum albumin-based neoglycoprotein (GalfNGP), carrying the multivalent Galf units, as a suitable ligand and high-avidity system for the recognition of GalfNeoLect which we successfully tested directly with the galactomannan spores of Aspergillus brasiliensis (ATCC 16404). Altogether, our results indicate that GalfNeoLect has the necessary versatility and plasticity to be used in both research and diagnostic lectin-based applications. Full article
(This article belongs to the Special Issue New Advances in Glycobiotechnology)
►▼ Show Figures

Graphical abstract

10 pages, 4974 KiB  
Article
Sodium-Doped 3-Amino-4-hydroxybenzoic Acid: Rediscovered Matrix for Direct MALDI Glycotyping of O-Linked Glycopeptides and Intact Mucins
by Shogo Urakami and Hiroshi Hinou
Int. J. Mol. Sci. 2023, 24(23), 16836; https://doi.org/10.3390/ijms242316836 - 28 Nov 2023
Viewed by 918
Abstract
3-Amino-4-hydroxybenzoic acid (AHB) was the first matrix identified by glycoprotein glycan analysis using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). However, compared to commonly used matrices, such as 2,5-dihydroxybenzoic acid (DHB), AHB is less efficient at glycan ionization and lacks the ability to ionize [...] Read more.
3-Amino-4-hydroxybenzoic acid (AHB) was the first matrix identified by glycoprotein glycan analysis using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). However, compared to commonly used matrices, such as 2,5-dihydroxybenzoic acid (DHB), AHB is less efficient at glycan ionization and lacks the ability to ionize other molecular species, such as peptides, and thus is no longer used. In this study, we focused on the glycan-selective ionization ability of AHB and its low-noise properties in the low-molecular-weight region, as we expected that these properties could be enhanced by adding sodium to AHB. Sodium-doped AHB (AHB/Na) selectively imparts sodium adduct ions onto O-glycan fragments generated by the in-source decay (ISD) of glycopeptides and glycoproteins containing O-glycans that occurs during intense laser irradiation, enabling direct O-glycan analysis. Furthermore, we demonstrated that it is possible to investigate the internal structure of each O-glycan fragment with pseudo-MS/MS/MS using the sodium adduct ion of the O-glycan-derived ISD fragments from an intact mucin mixture. Full article
(This article belongs to the Special Issue New Advances in Glycobiotechnology)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-2
Back to TopTop