Mechanism of multivalent glycoconjugate-lectin interaction: An update.

Lectins / chemistry Glycoconjugates / chemistry Glycoproteins / chemistry Polysaccharides Mucins
Calorimetry Glycan Glycosaminoglycan Lectin Multivalency Proteoglycan Thermodynamics

Journal

Advances in carbohydrate chemistry and biochemistry
ISSN: 2162-5530
Titre abrégé: Adv Carbohydr Chem Biochem
Pays: Netherlands
ID NLM: 0240537

Informations de publication

Date de publication:
2023
Historique:
medline: 20 11 2023
pubmed: 19 11 2023
entrez: 18 11 2023
Statut: ppublish

Résumé

Lectins are predominantly oligomeric proteins with several binding sites per molecule. Glycoconjugates are their natural ligands, which often possess multiple binding epitopes. Thus, lectin-glycoconjugate interactions are mostly multivalent in nature. The mechanism of multivalent binding is fundamentally different from those described for monovalent interactions in textbooks and research papers. Over the years, binding studies that make use of different lectins and a variety of multivalent glycoconjugate ligands were conducted in order to understand the underlying principles of multivalency. Starting with seemingly simple synthetic multivalent analogs, systematic studies were carried out using natural glycoconjugate ligands with increasing valency and complexity. Those ligands included multivalent glycoproteins, polyvalent polysaccharides, including glycosaminoglycans, as well as supra-valent mucins and proteoglycans. Models and mechanisms of multivalent binding derived from quantitative data are summarized in the present updated review.

Identifiants

DOI: 10.1016/bs.accb.2023.10.004 PMID: 37979977
pubmed: 37979977
pii: S0065-2318(23)00004-5
doi: 10.1016/bs.accb.2023.10.004
pii:
doi:

Substances chimiques

Lectins 0
Glycoconjugates 0
Glycoproteins 0
Polysaccharides 0
Mucins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1-21

Informations de copyright

Copyright © 2023 Elsevier Inc. All rights reserved.

Auteurs

Tarun K Dam (TK)

Laboratory of Mechanistic Glycobiology, Department of Chemistry, Michigan Technological University, Houghton, MI, United States; Health Research Institute, Michigan Technological University, Houghton, MI, United States. Electronic address: tkdam@mtu.edu.

Olivia Hohman (O)

Laboratory of Mechanistic Glycobiology, Department of Chemistry, Michigan Technological University, Houghton, MI, United States.

Lucas Sheppard (L)

Laboratory of Mechanistic Glycobiology, Department of Chemistry, Michigan Technological University, Houghton, MI, United States.

C Fred Brewer (CF)

Department of Molecular Pharmacology, Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, United States.

Purnima Bandyopadhyay (P)

Laboratory of Mechanistic Glycobiology, Department of Chemistry, Michigan Technological University, Houghton, MI, United States.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Lectines › Mechanism of multivalent glycoconjugate-lectin...
questionsmedicales.fr › Glucides › Glycoconjugués › Mechanism of multivalent glycoconjugate-lectin...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Glycoprotéines › Mechanism of multivalent glycoconjugate-lectin...
questionsmedicales.fr › Glucides › Polyosides › Mechanism of multivalent glycoconjugate-lectin...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Glycoprotéines › Mucoprotéines › Mucines › Mechanism of multivalent glycoconjugate-lectin...