化学
人血清白蛋白
半胱氨酸
钆
硫醇
立体化学
结合位点
共价键
生物化学
有机化学
酶
作者
Bhumasamudram Jagadish,Gerald P. Guntle,Dan Zhao,Vijay Gokhale,Tarik J. Ozumerzifon,Ali M. Ahad,Eugene A. Mash,Natarajan Raghunand
摘要
The synthesis and structure–activity relationships of a homologous series of 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid gadolinium(III) complexes bearing thiol-terminated alkyl side chains from three to nine carbons in length are reported. The observed binding with human serum albumin (HSA) of the compounds having C-3 through C-7 side chain lengths was inhibited by homocysteine in a manner consistent with single-site binding. The observed binding with HSA of the compounds having C-8 and C-9 side chain lengths was only partly inhibited by homocysteine, consistent with multisite binding. The binding affinity of the C-7 compound could be related to the HSA oxidation state. 2D 1H–1H NMR TOCSY provided evidence of covalent binding of the europium analog of the C-6 compound to HSA-Cys34. The longitudinal water-proton MRI relaxivities of the gadolinium complexes at 7 T increased upon binding to HSA. On the basis of these results, the C-6 and C-7 compounds were identified as promising redox-sensitive MRI contrast agents.
科研通智能强力驱动
Strongly Powered by AbleSci AI