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Abstract
The interactions between bovine serum albumin (BSA) and polymer [poly(METAC-co-NIPAm-co-Tb(AA)3Phen·H2O), denoted as PMNTb] containing terbium has been investigated with fluorescence spectroscopy, zeta-potential and size measurements, and transmission electron microscopy (TEM). PMNTb was found to interact with BSA through the electrostatic interaction, and it quenches the fluorescence of BSA based on the static quenching mechanism. The distance between PMNTb and BSA was estimated to be 1.9 nm based on Föster’s theory. The fluorescence intensity of PMNTb at 547 nm increased dramatically in the presence of BSA. In addition, the zeta-potential results confirmed the electrostatic interaction between BSA and PMNTb. Different morphologies of PMNTb/BSA complex were also observed with TEM.