Interactions of some phenylindanedione anticoagulants with human serum albumin.
This study enabled us, to define the quantitative parameters of the interactions which give rise to the formation of complexes between five phenylindanediones and albumin or polymethacryate. The existence of three attachment sites were demonstrated, by which these ligands are bound to the macromolecule. The results from the thermodynamic study of this phenomenon, together with the information supplied by; various spectroscopic methods; the formation of a complex between a synthetic polymer carrying amine functions, and the study of ligands in the presence of surfactant, were all in agreement. Furthermore, a significant correlation between the association constant and physiochemical parameters lipophilic character and acidity was obtained, leading to the conclusion that; the interactions permitting the formation of the complexes between albumin and the five anionic ligands seem to be principally hydrophobic and, to a lesser degree, electrostatic. The latter only occurred in a particular medium at sites which were mainly hydrophobic.
D000925:Anticoagulants / Q000378:metabolism*; D001665:Binding Sites; D006801:Humans; D008024:Ligands; D010630:Phenindione / Q000378:metabolism*; D011108:Polymers / Q000378:metabolism; D012709:Serum Albumin / Q000378:metabolism*; D013057:Spectrum Analysis; D013816:Thermodynamics
D000925:Anticoagulants; D008024:Ligands; D011108:Polymers; D012709:Serum Albumin; D010630:Phenindione