Propafenone binding interaction with human α1-acid glycoprotein: Assessing experimental design and data evaluation

Enantioselective plasma protein binding of propafenone: Mechanism, drug interaction, and species difference

“…which agree with previous reports for PPF racemate. 3,6 In this study, the S-PPF exhibited higher protein binding than the R-PPF either incubated with the single enantiomer or with the racemate. From the Scatchard curve, each of PPF enantiomer interacted with at least two classes of binding sites: one with high-affinity and small binding capacity, the other with low-affinity and high-binding capacity.…”

“…Therefore, the results may not be so indicative for enantiomers. Both of Oravcová et al 5 and Š olté s et al 6 measured the binding of PPF enantiomers with AGP by using a drug solution saturating a nonchiral high-performance size exclusion column. They observed two classes of binding sites: one with high affinity, the other with low-affinity and high capacity, which is the same to our results.…”

“…The observations indicated that competitive interactions between PPF enantiomers occurred at the high-affinity binding site. 4 rac-PPF 0.79 1.31 3 10 5 n 2 5 0.20 K 2 5 1.67 3 10 7 Oravcová et al 5 S-PPF 0.99 6 0.08 (8.93 6 1.82) 3 10 5 (1.06 6 0.09) 3 10 4 R-PPF 1.34 6 0.09 (6.18 6 0.93) 3 10 5 (6.87 6 0.72) 3 10 3 Š olté s et al 6 S-PPF 0.98 6 0.08 (9 6 1.88) 3 10 5 (1.07 6 0.09) 3 10 4 R-PPF 1.33 6 0.09 (6.2 6 0.94) 3 10 5 (6.9 6 0.72) 3 10 3 There are several types of interactions between small ligand and macromolecule, including hydrophobic bond, hydrogen bond, van der waals force, electrostatic action, and so on. Different drugs or different enantiomers of chiral drugs may have dissimilar types of interaction with proteins.…”

“…Some work has been reported about the binding of PPF in serum 3 and AGP, [4][5][6] as well as the species differences. 7 However, there are no reports about the binding of PPF with HSA and the binding mode with AGP.…”

Reversible binding interactions between the tryptophan enantiomers and albumins of different animal species as determined by novel high performance liquid chromatographic methods: an attempt to localize the D- and L-tryptophan binding sites on the human serum albumin polypeptide chain by using protein fragments

“…6 Consequently, it is important to determine the reversible binding interactions between particular plasma proteins and individual drug enantiomers. [7][8][9] This study describes some of the consequences which should be taken into account when the method of Hummel and Dreyer is used with two enantiomeric species run in the HPLC mobile phase.…”