Apr 30, 2020

Biophysical interaction of levothyroxine with bovine serum albumin: a spectroscopic assay

BioRxiv : the Preprint Server for Biology
Monica FlorescuM. David

Abstract

The binding mechanism and affinity of the interaction between levothyroxine (LT4) and bovine serum albumin (BSA) were investigated, both in solution using UV-Vis, Fourier-transform infrared spectroscopy (FT-IR), fluorescence and fluorescence resonance energy transfer (FRET), as well as by Surface Plasmon Resonance (SPR) with BSA confined to a gold-coated chips. Quenching of BSA fluorescence by LT4 combined with UV-Vis spectroscopy shows a ground-state complex formation that may be accompanied by a nonradiative energy transfer process. FT-IR revealed the changes induced by LT4 in the secondary structure of BSA molecules, due to the partial unfolding of BSA native structure upon LT4 binding. Scatchard approach allowed the determination of the binding constant Kb (5.12 x 106 M-1) and the equilibrium dissociation constant Kd (19.5 x 10-6 M) which suggest a moderate binding, as well as the thermodynamic parameters, which correspond to an enthalpic process (-51.99 kJ mol-1), driven mainly by hydrogen bonds and van der Waals forces. Using SPR, first, the confinement of BSA onto the chip gold surface was optimized towards LT4 binding. Second, the binding affinity of LT4 with BSA was characterized using the Hill-Langmuir equation, which...Continue Reading

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