A biophysical approach to formulation development: drug-plasma protein interaction

Fernandes, Eduarda; Soares, Telma; Oliveira, M.E.C.D. Real; Lopes, Carla Martins; Lúcio, Marlene

http://hdl.handle.net/10284/8998

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Authors

Fernandes, Eduarda

Soares, Telma

Oliveira, M.E.C.D. Real

Lopes, Carla Martins

Lúcio, Marlene

Abstract(s)

In this work, the binding constant of ACV to human serum albumin was determined by binding isotherms. Nonlinear leastsquares best fit to intrinsic fluorescence quenching effect of the drug was used to determine the association constants between drug and the serum protein at one affinity binding site (Kb=1.79x103 M-1). A red shift of the fluorescent spectra confirms association. Thermodynamic parameters for the binding indicated that electrostatic interactions are predominantly involved in the binding of this drug to human serum albumin. This was further confirmed by electrophoretic and dynamic light scattering, where a progressive charge neutralization of the protein was followed by an increase of the size of albumin-drug complex.