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Glyco-AuNP

The adhesion protein FimH mediates the attachment of uropathogenic E. coli strains with the host cell glycocalyx and specifically recognizes mannosylated structures. In 2002, Lin et al. first demonstrated that the glyco-AuNP can be used as a probe for staining the binding protein on the cell surface through carbohydrate-receptor interactions [67], Man-AuNPs were used to visualize the FimH adhesins on the type I pili of E. coli via transmission electron microscopy. [Pg.441]

Glyco-AuNPs have been shown to simultaneously enrich and isolate proteins from a very dilute solution with minimal sample handling [84], AuNPs offer an additional advantage in that bound proteins can be identified directly by mass spectrometry without the elution of the captured protein because of the electrical conductivity of the nanoparticles. Lin et al. previously prepared Gal-AuNP and Pk-AuNP and... [Pg.444]


See other pages where Glyco-AuNP is mentioned: [Pg.427]    [Pg.429]    [Pg.433]    [Pg.434]    [Pg.435]    [Pg.427]    [Pg.429]    [Pg.433]    [Pg.434]    [Pg.435]   
See also in sourсe #XX -- [ Pg.427 , Pg.429 , Pg.433 , Pg.434 , Pg.441 , Pg.444 ]




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