TY - JOUR
A2 - Eckhardt, Craig J.
AU - Yue, Qiaoli
AU - Shen, Tongfei
AU - Wang, Changna
AU - Gao, Chaohui
AU - Liu, Jifeng
PY - 2012
DA - 2012/07/15
TI - Study on the Interaction of Bovine Serum Albumin with Ceftriaxone and the Inhibition Effect of Zinc (II)
SP - 284173
VL - 2012
AB - The mechanism of the interaction between bovine serum albumin (BSA) and ceftriaxone with and without zinc (II) (Zn2+) was studied employing fluorescence, ultraviolet (UV) absorption, circular dichroism (CD), and synchronous fluorescence spectral methods. The intrinsic fluorescence of BSA was quenched by ceftriaxone in a static quenching mode, which was authenticated by Stern-Volmer calculations. The binding constant, the number of binding sites, and the thermodynamic parameters were obtained, which indicated a spontaneous and hydrophobic interaction between BSA and ceftriaxone regardless of Zn2+. Changes in UV absorption, CD, and synchronous fluorescence spectral data are due to the microenvironment of amide moieties in BSA molecules. In the BSA-ceftriaxone-Zn2+ system, Zn2+ must first interact with ceftriaxone forming a complex, which inhibits BSA binding to ceftriaxone. The present work uses spectroscopy to elucidate the mechanism behind the interaction between BSA and ceftriaxone in the presence and absence of Zn2+. The BSA and ceftriaxone complex provides a model for studying drug-protein interactions and thus may further facilitate the study of drug metabolism and transportation.
SN - 1687-9449
UR - https://doi.org/10.1155/2012/284173
DO - 10.1155/2012/284173
JF - International Journal of Spectroscopy
PB - Hindawi Publishing Corporation
KW -
ER -