Molecular interaction of human serum albumin with paracetamol: spectroscopic and molecular modeling studies.
The interaction between paracetamol and human serum albumin (HSA) under physiological conditions has been investigated by fluorescence, circular dichroism (CD) and docking. Fluorescence data revealed that the fluorescence quenching of HSA by paracetamol was the result of the formed complex of HSA-paracetamol, and the binding constant (K(a)) and binding number obtained is 1.3 x 10(4) at 298 K and 2, respectively for the primary binding site. Circular dichorism spectra showed the induced conformational changes in HSA by the binding of paracetamol. Moreover, protein-ligand docking study indicated that paracetamols (two paracetamols bind to HSA) bind to residues located in the subdomain IIIA.
Daneshgar
Parandis
P
Center of Excellence in Electrochemistry, University of Tehran, Tehran, Iran.
Moosavi-Movahedi
Ali Akbar
AA
Norouzi
Parviz
P
Ganjali
Mohammad Reza
MR
Madadkar-Sobhani
Armin
A
Saboury
Ali Akbar
AA
D000082:Acetaminophen / Q000737:chemistry* / Q000378:metabolism*; D018712:Analgesics, Non-Narcotic / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D002942:Circular Dichroism; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D018712:Analgesics, Non-Narcotic; D012709:Serum Albumin; D000082:Acetaminophen