2022
DOI: 10.1016/j.colsurfb.2022.112367
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Oxidation state of graphene oxide nanosheets drives their interaction with proteins: A case of bovine serum albumin

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Cited by 7 publications
(1 citation statement)
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“…Conjugation of GO with BSA protein and FITC fluorophore produced better dispersibility in working medium (RPMI) of GO and enabled us to monitor cellular uptake and reduce nanosheet thickness. In addition to the morphological-topographic result, obtained by AFM, the decrease in fluorescence due to quenching confirmed the formation of a stable composite GO-BSA-FITC; it was known GO nanosheets had a great adsorption capacity for proteins like BSA [36] and functionalization with serum proteins improved uptake and biocompatibility [37].…”
Section: Discussionmentioning
confidence: 71%
“…Conjugation of GO with BSA protein and FITC fluorophore produced better dispersibility in working medium (RPMI) of GO and enabled us to monitor cellular uptake and reduce nanosheet thickness. In addition to the morphological-topographic result, obtained by AFM, the decrease in fluorescence due to quenching confirmed the formation of a stable composite GO-BSA-FITC; it was known GO nanosheets had a great adsorption capacity for proteins like BSA [36] and functionalization with serum proteins improved uptake and biocompatibility [37].…”
Section: Discussionmentioning
confidence: 71%