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Fabrication of an Oriented Fc‐Fused Lectin Microarray through Boronate Formation
Author(s) -
Chen MuLin,
Adak Avijit Kumar,
Yeh NaiChia,
Yang WenBin,
Chuang YungJen,
Wong ChiHuey,
Hwang KuoChu,
Hwu JihRu Reuben,
Hsieh ShihLiang,
Lin ChunCheng
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200803377
Subject(s) - streptavidin , lectin , chemistry , covalent bond , biotinylation , biotin , moiety , fusion protein , biochemistry , microarray , staining , polysaccharide , recombinant dna , stereochemistry , biology , organic chemistry , gene , gene expression , genetics
A stable, covalent, and highly active protein microarray was created through the formation of cyclic esters between surface boronic acids and the carbohydrate moiety of a fusion protein, Fc‐dectin‐1 (see picture). A biotin‐labeled polysaccharide was used as a probe to investigate the binding activity of the protein. Staining of the product array with streptavidin‐Cy3 revealed the effectiveness of this immobilization strategy.