Abstract
Objective: Since structural changes of adsorbed protein are necessary for cellular uptake of nanoparticles (NPs) it is of prime importance to know about structural changes of bovine serum albumin (BSA) when it interacts with CuO NPs–a potential new antitumor drug.Methods: CuO NPs prepared by sol-gel technique were characterized by x-ray diffraction (XRD) and tunneling electron microscope (TEM) techniques. The conformational changes induced by CuO NPs on BSA were studied by various spectroscopic techniques such as steady state and time-resolved fluorescence measurements. The changes in fluorescence emission parameters such as fluorescence intensity, fluorescence emission maximum and lifetimes of fluorescent residues in BSA were studied.Results: XRD analysis showed the average particle size as 32 nm. The TEM micrograph showed particles of different size varying from 10 to 45 nm. Fluorescence quenching was confirmed due to a decrease in fluorescence intensity of CuO NPs–BSA complex. The analysis of lifetime measurements indicated BSA contained two tryptophan (trp) residues that fluoresced in different environments. Static quenching mechanism was confirmed by time-resolved measurements when BSA interacted with CuO NPs.Conclusion: Minor structural changes of BSA protein were observed during the interaction studies.
Highlights
Nanotechnology holds a huge promise for the design and development of many types of novel products with its potential medical applications on early disease detection, treatment and prevention [1,2,3,4]
All the existing diffraction peaks in x-ray diffraction (XRD) profile are in good agreement with standard JCPDS data (File no. 05-661)
Static quenching mechanism was confirmed by time-resolved measurements when bovine serum albumin (BSA) interacted with colloidal ZnO nps [35], SnO2 nps [32], TiO2 nps [36] and no significant change in average lifetime of trp residues with gold NPs [37]
Summary
Nanotechnology holds a huge promise for the design and development of many types of novel products with its potential medical applications on early disease detection, treatment and prevention [1,2,3,4]. NPs large functional surface area allows them to bind absorb and carry other compounds [5]. Copper compounds have been used to treat cancer and several diseases for thousands of years [6]. In vitro and in vivo studies showed that metal oxide NPs can directly kill tumor cells [7]. CuO NPs have many advantages such as simple preparation procedure, long-term stability, and anticancer properties and showed a strong affinity to bind blood carrier proteins [8, 9]. BSA is a good model to study protein conformational changes due to its wide range of physiological functions [10], an ideal protein for intrinsic fluorescence measurements [11], wellcharacterized structure and property and readily undergoes conformational changes [12, 13]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: International Journal of Pharmacy and Pharmaceutical Sciences
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
