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Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin
- Maity, Arnab, Pal, Uttam, Chakraborty, Brotati, Sengupta, Chaitrali, Sau, Abhishek, Chakraborty, Swatadipta, Basu, Samita
- International journal of biological macromolecules 2019 v.137 pp. 483-494
- absorption, blood serum, bovine serum albumin, carbon, circular dichroism spectroscopy, drugs, energy transfer, fluorescence, fluorescent dyes, human serum albumin, moieties, photochemistry, ruthenium, transport proteins, tryptophan, wavelengths
- The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells.