Abstract
We conducted an infrared spectroscopic study of the concentration-dependent conformational changes of bovine serum albumin (BSA) and transferrin (Tf) on ZnO nanoparticles (NPs) functionalized with self-assembled monolayers. The ZnO NPs used as a platform for protein conjugation were characterized by their UV absorption spectroscopy, X-ray diffraction (XRD), and transmission electron microscopy (TEM). Self-assembled thin films of 16-phosphonohexadecanoic acid (16-PHDA) for anchoring proteins onto ZnO surfaces were examined by diffuse reflectance infrared Fourier-transform (DRIFT) spectroscopy. The presence of the strong ν(CO) band at ∼1700cm−1, along with the significant changes of the P–OH, P–O, and PO bands at 930–1215cm−1 in the DRIFT spectra, indicate that at least some of the 16-PHDA appeared to adsorb onto the ZnO surfaces via its phosphonic acid group. Protein-ZnO nanoparticle (NP) conjugates were assembled by a 1-ethyl-3-[3-dimethylaminopropyl]carbodiimide hydrochloride (EDC) coupling reaction. The protein conjugations of bovine serum albumin (BSA) and transferrin (Tf) were verified by identifying their amide bands in the infrared spectra. By referring to the peak analysis of the amide I bands, different surface-induced conformational changes of the two proteins could be observed upon their adsorption on ZnO.
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 callDisclaimer: 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.
