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• W2122333326 startingPage "22098" @default.
• W2122333326 abstract "The binding of proteins to a nanostructure often alters protein secondary and tertiary structures. However, the main physical mechanisms that elicit protein conformational changes in the presence of the nanostructure have not yet been fully established. Here we performed a comprehensive spectroscopic study to probe the interactions between bovine serum albumin (BSA) and carbon-based nanostructures of graphene and single-walled carbon nanotubes (SWNTs). Our results showed that the BSA “corona” acted as a weak acceptor to facilitate charge transfer from the carbon nanostructures. Notably, we observed that charge transfer occurred only in the case of SWNTs but not in graphene, resulting from the sharp and discrete electronic density of states of the former. Furthermore, the relaxation of external α-helices in BSA secondary structure increased concomitantly with the charge transfer. These results may help guide controlled nanostructure–biomolecular interactions and prove beneficial for developing novel drug delivery systems, biomedical devices, and engineering of safe nanomaterials." @default.
• W2122333326 created "2016-06-24" @default.
• W2122333326 creator A5002417481 @default.
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• W2122333326 date "2012-10-09" @default.
• W2122333326 modified "2023-09-27" @default.
• W2122333326 title "Evidence for Charge-Transfer-Induced Conformational Changes in Carbon Nanostructure–Protein Corona" @default.
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• W2122333326 doi "https://doi.org/10.1021/jp3085028" @default.
• W2122333326 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3519440" @default.
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• W2122333326 hasPublicationYear "2012" @default.
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