Fluorescence quenching studies on binding fluoreno-9-spiro-oxazolidinedione to human serum albumin.
Human serum albumin fluorescence quenching by fluorene-9-spiro-oxazolidinedione has been analyzed as a function of temperature. Such temperature dependence suggests that the mechanism of the quenching process is static in origin. This type of quenching implies that a non-fluorescent complex between oxazolidinedione and serum albumin has been formed and following the Stern-Volmer relationship we have calculated the binding constant. Thermodynamic parameters were also determined. The positive and large values of entropy and the negative value for enthalpy suggest that both hydrophobic and electrostatic interactions may play an important role in the stabilization of the complex. Finally, the irreversible changes in the spectral properties of HSA are interpreted in binding terms.
Gonzalez-Jimenez
J
J
Departamento de Quimica-Fisica Farmaceutica, Facultad de Farmacia, Universidad Complutense, Ciudad Universitaria, Madrid, Spain.
Jacquotte
H
H
Cayre
I
I
D000465:Algorithms; D005449:Fluorenes / Q000493:pharmacokinetics*; D005453:Fluorescence; D006801:Humans; D010080:Oxazoles / Q000493:pharmacokinetics*; D023303:Oxazolidinones; D012709:Serum Albumin / Q000378:metabolism*; D013696:Temperature
D005449:Fluorenes; D010080:Oxazoles; D023303:Oxazolidinones; D012709:Serum Albumin; C078228:fluorene-9-spiro-5'-oxazolidinedione