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Multivalency in Protein–Carbohydrate Recognition

  • Reference work entry
Glycoscience

Abstract

The binding of proteins to individual glycoconjugates is often weak. In physiological settings, carbohydrate–protein interactions often benefit from multivalency—multiple copies of the carbohydrate epitope engage with multiple copies of a carbohydrate–binding protein. This mode of molecular recognition is especially important in cell adhesion because the individual interactions need to be kinetically labile yet highly specific. This review discusses why protein–carbohydrate interactions are especially well-suited for multivalent binding, the binding modes and energetic forces that underlie multivalent protein–carbohydrate complexes, and the utility of multivalent carbohydrate derivatives for exploring multivalent binding and inhibiting physiologically and medically important protein–carbohydrate interactions.

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Abbreviations

ASGR:

asialoglycoprotein receptor

ATRP:

atom-transfer radical polymerization

bFGF:

basic fibroblast growth factor

BSA:

bovine serum albumin

ConA:

concanavalin A 

ELLA:

enzyme-linked lectin inhibition assay

EcorL:

Erythrina corallodendrum

FRET:

Förster resonance energy transfer

LOL I:

Lathyrus ochrus lectin I

LT:

labile enterotoxin

LFA:

Limax flavus

MBPs:

mannose-binding proteins

PAMAM:

polyamidoamine

ROMP:

ring-opening metathesis polymerization

SLT:

Shiga-like toxins

SPR:

surface plasmon resonance

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Kiessling, L., Young, T., Gruber, T., Mortell, K. (2008). Multivalency in Protein–Carbohydrate Recognition. In: Fraser-Reid, B.O., Tatsuta, K., Thiem, J. (eds) Glycoscience. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-30429-6_64

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