title: Impact of halogen substituents on interactions between 2-phenyl-2,3-dihydroqulinazolin-4(1H)-one derivatives and human serum albumin.
abstract: A novel type of 2-(un)substituted phenyl-2,3-dihydroquinazolin-4(1H)-one (DQL) derivatives were designed and synthesized to study the impact of halogen substituents on interactions between DQL and human serum albumin (HSA) by comparison methodology. The interactions between DQL and HSA were studied by fluorescence spectroscopy. The intrinsic fluorescence of human serum albumin was quenched by DQL through a static quenching mechanism. Site marker competitive experiments showed that DQL bound to HSA in site II (subdomain IIIA). The binding constants, the numbers of binding sites and the thermodynamic parameters were measured too. The results indicated that the interactions were spontaneous, mainly through hydrophobic forces, and the substitution by halogen atoms in the benzene ring could increase the interactions between DQL and HSA. Furthermore, the binding affinity was enhanced gradually with the increasing of halogen atomic number.
authors.affiliation: Department of Applied Chemistry, China Agricultural University, Beijing 100193, China.
authors.forename: Feng
authors.initials: F
authors.lastname: Liu
authors.forename: Yi
authors.initials: Y
authors.lastname: Wang
authors.forename: Cong
authors.initials: C
authors.lastname: Lv
authors.forename: Lei
authors.initials: L
authors.lastname: Wang
authors.forename: Junjun
authors.initials: J
authors.lastname: Ou
authors.forename: Min
authors.initials: M
authors.lastname: Wang
authors.forename: Shangzhong
authors.initials: S
authors.lastname: Liu
mesh_terms: D001665:Binding Sites; D005453:Fluorescence; D006219:Halogens / Q000737:chemistry*; D006801:Humans; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods; D013329:Structure-Activity Relationship; D013816:Thermodynamics
chemical_list: D006219:Halogens; D012709:Serum Albumin