En route to photoaffinity labeling of the bacterial lectin FimH
نویسندگان
چکیده
منابع مشابه
En route to photoaffinity labeling of the bacterial lectin FimH
Mannose-specific adhesion 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-specific adhesion is not yet fully understood, it is of i...
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15 صفحه اولThe mechanism of photoaffinity labeling.
Photoaffinity labeling is a recently introduced method for covalently binding chemical tags to the active sites of protein molecules, which is potentially capable of very great specificities of labeling. A labeling reagent is used that is converted by photolysis to an extremely reactive intermediate. According to the expected mechanism, the reagent molecules that are specifically and reversibly...
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The Amadori rearrangement was employed for the synthesis of C-glycosyl-type D-mannoside analogues, namely 1-propargylamino- and 1-phenylamino-1-deoxy-α-D-manno-heptopyranose. They were investigated as ligands of type 1-fimbriated E. coli bacteria by means of molecular docking and bacterial adhesion studies. It turns out that Amadori rearrangement products have a limited activity as inhibitors o...
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ژورنال
عنوان ژورنال: Beilstein Journal of Organic Chemistry
سال: 2010
ISSN: 1860-5397
DOI: 10.3762/bjoc.6.91