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Molecules
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Oligosaccharides and Glyco-Conjugates II
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Oligosaccharides and Glyco-Conjugates II

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

Deadline for manuscript submissions: closed (31 August 2020) | Viewed by 10230

Special Issue Editors

Prof. Dr. Marco Terreni

E-Mail Website
Guest Editor
Department of Drug Sciences, School of Pharmacy, University of Pavia, Via Taramelli 12, 27100 Pavia, Italy
Interests: syndetic organic chemistry; medicinal chemistry; chemical biology; protein engineering; biocatalysis
Special Issues, Collections and Topics in MDPI journals
Dr. Teodora Bavaro

E-Mail Website
Guest Editor
Department of Drug Sciences, University of Pavia, Viale Taramelli 12, 27100 Pavia, Italy
Interests: chemoenzymatic synthesis; medicinal chemistry; biocatalysis; protein engineering
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Glycans play many important roles in biological processes and in pathology. Accordingly, different oligosaccharide derivatives are being increasingly investigated in medicinal chemistry targeting bioprocesses mediated by protein–oligosaccharide or oligosaccharide–oligosaccharide interaction.
For this purpose, well-defined oligosaccharides can be obtained by chemical and/or enzymatic approaches, but their synthesis is still challenging. Novel and efficient synthetic procedures for glycoconjugate compounds need to be developed and optimized. Moreover, an alternative and suitable strategy for the development of efficient glycan-based products must be combined with analytical technologies to assess the exact characterization/identification of the biopharmaceuticals.
The present Special Issue is the second that we have proposed and aims at covering emerging methods for oligosaccharide synthesis, glycoconjugate assembly (chemical, enzymatic and chemoenzymatic methodologies) and biological screening, and highlight innovative strategies for glyco-derivative based drug design. In addition, new methods for the analytical and biological characterization of oligosaccharides and glycoconjugates are welcomed for submission to this Special Issue.

Prof. Dr. Marco Terreni
Dr. Teodora Bavaro
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

  • Oligosaccharides
  • Glycoproteins
  • Glycopeptides
  • Glycolipids
  • Synthetic methodologies
  • Structure characterization
  • Analysis
  • Biological activity
  • Drug discovery and development

Published Papers (3 papers)

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Research

12 pages, 5434 KiB  
Article
Synthesis and Antibody Binding Studies of Schistosome-Derived Oligo-α-(1-2)-l-Fucosides
by Michael R. Harvey, Fabrizio Chiodo, Wouter Noest, Cornelis H. Hokke, Gijsbert A. van der Marel and Jeroen D.C. Codée
Molecules 2021, 26(8), 2246; https://doi.org/10.3390/molecules26082246 - 13 Apr 2021
Cited by 1 | Viewed by 1863
Abstract
Schistosomiasis is caused by blood-dwelling parasitic trematodes of the genus Schistosoma and is classified by the WHO as the second most socioeconomically devastating parasitic disease, second only to malaria. Schistosoma expresses a complex array of glycans as part of glycoproteins and glycolipids that [...] Read more.
Schistosomiasis is caused by blood-dwelling parasitic trematodes of the genus Schistosoma and is classified by the WHO as the second most socioeconomically devastating parasitic disease, second only to malaria. Schistosoma expresses a complex array of glycans as part of glycoproteins and glycolipids that can be targeted by both the adaptive and the innate part of the immune system. Some of these glycans can be used for diagnostic purposes. A subgroup of schistosome glycans is decorated with unique α-(1-2)-fucosides and it has been shown that these often multi-fucosylated fragments are prime targets for antibodies generated during infection. Since these α-(1-2)-fucosides cannot be obtained in sufficient purity from biological sources, we set out to develop an effective route of synthesis towards α-(1-2)-oligofucosides of varying length. Here we describe the exploration of two different approaches, starting from either end of the fucose chains. The oligosaccharides have been attached to gold nanoparticles and used in an enzyme-linked immunosorbent assay ELISA and a microarray format to probe antibody binding. We show that binding to the oligofucosides of antibodies in sera of infected people depends on the length of the oligofucose chains, with the largest glycans showing most binding. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates II)
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24 pages, 1468 KiB  
Article
Developing a Library of Mannose-Based Mono- and Disaccharides: A General Chemoenzymatic Approach to Monohydroxylated Building Blocks
by Lisa Tanzi, Marina Simona Robescu, Sara Marzatico, Teresa Recca, Yongmin Zhang, Marco Terreni and Teodora Bavaro
Molecules 2020, 25(23), 5764; https://doi.org/10.3390/molecules25235764 - 07 Dec 2020
Cited by 6 | Viewed by 2648
Abstract
Regioselective deprotection of acetylated mannose-based mono- and disaccharides differently functionalized in anomeric position was achieved by enzymatic hydrolysis. Candida rugosa lipase (CRL) and Bacillus pumilus acetyl xylan esterase (AXE) were immobilized on octyl-Sepharose and glyoxyl-agarose, respectively. The regioselectivity of the biocatalysts was affected [...] Read more.
Regioselective deprotection of acetylated mannose-based mono- and disaccharides differently functionalized in anomeric position was achieved by enzymatic hydrolysis. Candida rugosa lipase (CRL) and Bacillus pumilus acetyl xylan esterase (AXE) were immobilized on octyl-Sepharose and glyoxyl-agarose, respectively. The regioselectivity of the biocatalysts was affected by the sugar structure and functionalization in anomeric position. Generally, CRL was able to catalyze regioselective deprotection of acetylated monosaccharides in C6 position. When acetylated disaccharides were used as substrates, AXE exhibited a marked preference for the C2, or C6 position when C2 was involved in the glycosidic bond. By selecting the best enzyme for each substrate in terms of activity and regioselectivity, we prepared a small library of differently monohydroxylated building blocks that could be used as intermediates for the synthesis of mannosylated glycoconjugate vaccines targeting mannose receptors of antigen presenting cells. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates II)
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12 pages, 3432 KiB  
Article
Expanding the Reaction Space of Linkage-Specific Sialic Acid Derivatization
by Tamas Pongracz, Manfred Wuhrer and Noortje de Haan
Molecules 2019, 24(19), 3617; https://doi.org/10.3390/molecules24193617 - 08 Oct 2019
Cited by 18 | Viewed by 5212
Abstract
The human glycome is characterized by a high degree of sialylation, affecting, amongst others, cell–cell interactions and protein half-life. An established method for the linkage isomer-specific characterization of N-glycan sialylation is based on the linkage-specific derivatization of sialylated glycoconjugates, inducing ethyl esterification [...] Read more.
The human glycome is characterized by a high degree of sialylation, affecting, amongst others, cell–cell interactions and protein half-life. An established method for the linkage isomer-specific characterization of N-glycan sialylation is based on the linkage-specific derivatization of sialylated glycoconjugates, inducing ethyl esterification of α2,6-linked sialic acids and lactonization of α2,3-linked sialic acids. While the carboxylic acid activator and nucleophile used in this reaction received extensive investigation, the role of the catalyst was never thoroughly explored. A frequently used catalyst for the linkage-specific esterification of sialic acids is 1-hydroxybenzotriazole (HOBt). Here, a systematic evaluation was performed of five HOBt alternatives in combination with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) in ethanol for the linkage-specific derivatization of sialic acids. Derivatized glycans were analyzed by MALDI-TOF-MS and the catalyst performance was evaluated based on the completeness of the reactions and the linkage-specificity obtained. The use of both 6-Cl-HOBt and 6-CF3-HOBt resulted in high linkage-specificity and minimal byproduct formation, similar to the benchmark method using HOBt. Performing the reaction with these catalysts at neutral or acidic pH showed comparable efficiencies on both sialyllactose and complex-type N-glycans. The reported investigations resulted in an expansion of the reaction space for linkage-specific sialic acid derivatization. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates II)
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