Multivalent lectin-carbohydrate interactions energetics and mechanisms of binding.

Tarun K. Dam, Curtis F. Brewer

Research output: Contribution to journalArticle

75 Citations (Scopus)

Abstract

The biological signaling properties of lectins, which are carbohydrate-binding proteins, are due to their ability to bind and cross-link multivalent glycoprotein receptors on the surface of normal and transformed cells. While the crosslinking properties of lectins with multivalent carbohydrates and glycoproteins are relatively well understood, the mechanisms of binding of lectins to multivalent glycoconjugates are less well understood. Recently, the thermodynamics of binding of lectins to synthetic clustered glycosides, a multivalent globular glycoprotein, and to linear glycoproteins (mucins) have been described. The results are consistent with a dynamic binding mechanism in which lectins bind and jump from carbohydrate to carbohydrate epitope in these molecules. Importantly, the mechanism of binding of lectins to mucins is similar to that for a variety of protein ligands binding to DNA. Recent analysis also shows that high-affinity lectin-mucin crosslinking interactions are driven by favorable entropy of binding that is associated with the bind and jump mechanism. The results suggest that the binding of ligands to biopolymers, in general, may involve a common mechanism that involves enhanced entropic effects which facilitate binding and subsequent complex formation including enzymology.

Original languageEnglish (US)
Pages (from-to)139-164
Number of pages26
JournalAdvances in Carbohydrate Chemistry and Biochemistry
Volume63
DOIs
StatePublished - 2010
Externally publishedYes

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Lectins
Carbohydrates
Glycoproteins
Mucins
Crosslinking
Ligands
Biopolymers
Glycoconjugates
Entropy
Glycosides
Thermodynamics
Protein Binding
Epitopes
Molecules
DNA
Proteins

ASJC Scopus subject areas

  • Organic Chemistry
  • Biochemistry

Cite this

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abstract = "The biological signaling properties of lectins, which are carbohydrate-binding proteins, are due to their ability to bind and cross-link multivalent glycoprotein receptors on the surface of normal and transformed cells. While the crosslinking properties of lectins with multivalent carbohydrates and glycoproteins are relatively well understood, the mechanisms of binding of lectins to multivalent glycoconjugates are less well understood. Recently, the thermodynamics of binding of lectins to synthetic clustered glycosides, a multivalent globular glycoprotein, and to linear glycoproteins (mucins) have been described. The results are consistent with a dynamic binding mechanism in which lectins bind and jump from carbohydrate to carbohydrate epitope in these molecules. Importantly, the mechanism of binding of lectins to mucins is similar to that for a variety of protein ligands binding to DNA. Recent analysis also shows that high-affinity lectin-mucin crosslinking interactions are driven by favorable entropy of binding that is associated with the bind and jump mechanism. The results suggest that the binding of ligands to biopolymers, in general, may involve a common mechanism that involves enhanced entropic effects which facilitate binding and subsequent complex formation including enzymology.",
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AU - Dam, Tarun K.

AU - Brewer, Curtis F.

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