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Recent Opinion on Protein-Carbohydrate Interactions

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

Deadline for manuscript submissions: closed (31 December 2022) | Viewed by 2446

Special Issue Editors


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Guest Editor
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
Interests: oligosaccharides; glycoconjugates; self-assembling peptides/glycopeptides; carbohydrate-protein interactions

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Guest Editor
Department of Pharmaceutical Sciences, Universitat Basel, Basel, Switzerland
Interests: chemical and enzymatic synthesis of therapeutically promising oligosaccharides and mimetics thereof and the investigation of carbohydrate/protein interactions by NMR, surface plasmon resonance, microcalorimetry, and molecular modeling

Special Issue Information

Dear Colleagues,

In this issue, we would like to focus on the mechanisms and features of the interaction (thermodynamic and kinetic aspect) of carbohydrates and glycomimetics with proteins, and not simply on a descriptive presentation of the carbohydrate-binding specificity of a protein. We await articles discussing carbohydrate epitopes and protein paratopes, methods for localizing and investigating them, and approaches to applying this knowledge to the design of pharmacologically relevant epitopes or their mimetics. The spatial epitopes as well as architectures of recognition sites cognate to them (paratopes) are of particular interest. Here, we are not limited to canonical lectins and anti-glycan antibodies—articles on the glycan modules (motifs) of enzymes and other polyfunctional and modular proteins are also welcome. Oligosaccharides, polysaccharides, glycopeptides, and molecular clusters/patterns are the protagonists of our release.

Prof. Dr. Nicolai V. Bovin
Prof. Dr. Beat Ernst
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
  • polysaccharides
  • glycoconjugates
  • peptides/glycopeptides
  • carbohydrate-protein interactions
  • epitopes
  • molecular clusters/patterns

Published Papers (1 paper)

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Research

12 pages, 5717 KiB  
Article
Lactose and Galactose Promote the Crystallization of Human Galectin-10
by Yu-Fan Fu, Si-Cong Jiang, Zhong-Wei Zhang, Xin-Yue Yang, Zi-Lin Li, Jing Hu and Shu Yuan
Molecules 2023, 28(4), 1979; https://doi.org/10.3390/molecules28041979 - 19 Feb 2023
Viewed by 1929
Abstract
Galectin-10 (Gal-10) forms Charcot–Leyden crystals (CLCs), which play a key role in the symptoms of asthma and allergies and some other diseases. Gal-10 has a carbohydrate-binding site; however, neither the Gal-10 dimer nor the CLCs can bind sugars. To investigate the monomer–dimer equilibrium [...] Read more.
Galectin-10 (Gal-10) forms Charcot–Leyden crystals (CLCs), which play a key role in the symptoms of asthma and allergies and some other diseases. Gal-10 has a carbohydrate-binding site; however, neither the Gal-10 dimer nor the CLCs can bind sugars. To investigate the monomer–dimer equilibrium of Gal-10, high-performance size-exclusion chromatography (SEC) was employed to separate serial dilutions of Gal-10 with and without carbohydrates. We found that both the dimerization and crystallization of Gal-10 were promoted by lactose/galactose binding. A peak position shift for the monomer was observed after treatment with either lactose or galactose, implying that the polarity of the monomer was reduced by lactose/galactose binding. Further experiments indicated that alkaline conditions of pH 8.8 mimicked the lactose/galactose-binding environment, and the time interval between monomers and dimers in the chromatogram decreased from 0.8 min to 0.4 min. Subsequently, the electrostatic potential of the Gal-10 monomers was computed. After lactose/galactose binding, the top side of the monomer shifted from negatively charged to electrically neutral, allowing it to interact with the carbohydrate-binding site of the opposing subunit during dimerization. Since lactose/galactose promotes the crystallization of Gal-10, our findings implied that dairy-free diets (free of lactose/galactose) might be beneficial to patients with CLC-related diseases. Full article
(This article belongs to the Special Issue Recent Opinion on Protein-Carbohydrate Interactions)
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