New insight into the binding interaction of hydroxylated carbon nanotubes with bovine serum albumin

• Binding interaction of HO-MWCNTs with BSA was investigated.
• The binding site of HO-MWCNTs on BSA was near to domain II and domain I of BSA.
• HO-MWCNTs acted as a pusher to increase the rate of fibrillation of BSA.
• The ligand binding and unfolding of BSA were also affected by HO-MWCNTs.

In order to understand the effects of carbon nanotubes on the structural stability of proteins, the ligand-binding ability, fibrillation, and chemical denaturation of bovine serum albumin in the presence of a multi-walled hydroxylated carbon nanotubes (HO-MWCNTs) was characterized by UV–vis, circular dichroism, fluorescence spectroscopy and molecule modeling methods at the molecular level. The experiment results indicated that the fluorescence intensity of BSA was decreased obviously in presence of HO-MWCNTs. The binding interaction of HO-MWCNTs with BSA led to the secondary structure changes of BSA. This interaction could not only affect the ligand-binding ability of BSA, but also change the rate of fibrillation and denaturation of BSA. This work gave us some important information about the structures and properties of protein induced by carbon nanotubes.

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