Characterization of the Binding of the Finland Trityl Radical with Bovine Serum Albumin.

ABSTRACT: Understanding the interactions of trityl radicals with proteins is required to expand their biomedical applications. In this work, we demonstrate that the Finland trityl radical CT-03 binds to bovine serum albumin (BSA) in aqueous solution. Upon binding with BSA, CT-03 exhibits a much broader electron paramagnetic resonance (EPR) signal and this line broadening can be reversed by proteolysis of the BSA. The binding induces a red-shift of the maximal UV-Vis absorbance wavelength of CT-03 around 470 nm, likely due to localization of CT-03 in the relatively hydrophobic region of the protein. The interaction between CT-03 and BSA is driven by a hydrophobic interaction with an estimated binding constant of 2.18 ×10⁵ M^-1 at 298 K. Furthermore, only one CT-03 is bound to eac

SUBMITTER: Song Y 

PROVIDER: S-EPMC4527563 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature