Abstract
ABSTRACTIn the Tris-HCl buffer solution with pH = 7.4, the reaction mechanism of cefonicid sodium with bovine transferrin was investigated by multi-spectroscopic methods at different temperatures (298, 303, and 310 K). The results demonstrated that non-radiative energy transfer occurred between cefonicid sodium and bovine transferrin, which gradually quenched the fluorescence of bovine transferrin, and the quenching mechanism was a static quenching progress. During the quenching progress, the electrostatic force played a dominant role in this system, and the number of binding sites in the system was close to 1. Moreover, ultraviolet visible absorption spectroscopy and synchronous fluorescence spectroscopy showed that the structure of bovine transferrin was changed. The polarity around amino acid residues increased and the hydrophobicity decreased. Circular dichroism spectroscopy also showed that cefonicid sodium changed the secondary structure of bovine transferrin. However, the structure of the bovine transferrin was also predominantly α-helical even after binding to cefonicid sodium. The values of Hill’s coefficients were less than 1, indicating that drugs had negative cooperativity for subsequent ligands in the system.
Sign-in/Register to access full text options 
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.
