title: Molecular interaction of human serum albumin with paracetamol: spectroscopic and molecular modeling studies.
abstract: 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.
authors.affiliation: Center of Excellence in Electrochemistry, University of Tehran, Tehran, Iran.
authors.forename: Parandis
authors.initials: P
authors.lastname: Daneshgar
authors.forename: Ali Akbar
authors.initials: AA
authors.lastname: Moosavi-Movahedi
authors.forename: Parviz
authors.initials: P
authors.lastname: Norouzi
authors.forename: Mohammad Reza
authors.initials: MR
authors.lastname: Ganjali
authors.forename: Armin
authors.initials: A
authors.lastname: Madadkar-Sobhani
authors.forename: Ali Akbar
authors.initials: AA
authors.lastname: Saboury
mesh_terms: 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
chemical_list: D018712:Analgesics, Non-Narcotic; D012709:Serum Albumin; D000082:Acetaminophen