Beilstein J. Org. Chem.2015,11, 720–729, doi:10.3762/bjoc.11.82
protein receptors are formed to control cell–cell recognition, cell adhesion and related processes. The aim of this work is to shed light on the principles of complex formation between surface anchored carbohydrates and receptor surfaces by measuring the specificadhesion between surface bound mannose on
a concanavalin A (ConA) layer via poly(ethylene glycol)-(PEG)-based soft colloidal probes (SCPs). Special emphasis is on the dependence of multivalent presentation and density of carbohydrate units on specificadhesion. Consequently, we first present a synthetic strategy that allows for controlled
synthetic strategy allows for straightforward variation in grafting density and grafting length enabling the controlled presentation of mannose units on the PEG network. Finally we determined the specificadhesion of PEG-network-conjugated mannose units on ConA surfaces as a function of density and grafting
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Graphical Abstract
Figure 1:
SCP adhesion measurement sketch (top): A mannose-functionalized PEG-SCP sediments onto a Concanaval...
Beilstein J. Org. Chem.2010,6, 810–822, doi:10.3762/bjoc.6.91
, Uppsala Biomedical Center, SE-75124 Uppsala, Sweden 10.3762/bjoc.6.91 Abstract Mannose-specificadhesion of Escherichia coli bacteria to cell surfaces, the cause of various infections, is mediated by a fimbrial lectin, called FimH. X-ray studies have revealed a carbohydrate recognition domain (CRD) on
FimH that can complex α-D-mannosides. However, as the precise nature of the ligand–receptor interactions in mannose-specificadhesion is not yet fully understood, it is of interest to identify carbohydrate recognition domains on the fimbrial lectin also in solution. Photoaffinity labeling serves as an
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Graphical Abstract
Figure 1:
The photoaffinity technique allows the identification of ligand binding sites of a receptor protein...