Binding study of carbon dots to bovine serum albumin

Abstract

To increase the efficiency of carbon dots (C-dots), surface of C-dots were functionalized with bovine serum albumin (BSA). The synthesized C-dot were naturally luminescence and it has a high potential to be a biomarker in biomedical field. Bovine serum is a serum protein which were widely using in biosensor area. Therefore binding mechanisms between C-dots and BSA is important to be study. This research reported two binding methods between C-dots and BSA which is formation of covalent bond and adsorption on the surface of BSA. Ultraviolet-Visible and Fourier transformed infrared analysis shows the breaking and formation of amide bond. For the adsorption binding method, the carbonyl bond peak was still appeared after the surface was functionalized with BSA. Both the binding study shows the fluorescence properties with similar intensity. Therefore this research suggesting adsorption binding method is an environmental friendly and more favorable method.To increase the efficiency of carbon dots (C-dots), surface of C-dots were functionalized with bovine serum albumin (BSA). The synthesized C-dot were naturally luminescence and it has a high potential to be a biomarker in biomedical field. Bovine serum is a serum protein which were widely using in biosensor area. Therefore binding mechanisms between C-dots and BSA is important to be study. This research reported two binding methods between C-dots and BSA which is formation of covalent bond and adsorption on the surface of BSA. Ultraviolet-Visible and Fourier transformed infrared analysis shows the breaking and formation of amide bond. For the adsorption binding method, the carbonyl bond peak was still appeared after the surface was functionalized with BSA. Both the binding study shows the fluorescence properties with similar intensity. Therefore this research suggesting adsorption binding method is an environmental friendly and more favorable method.