title: [Influence of albumin on the spectroscopic properties and existence state of mono-substituted phthalocyanine zinc (II)].
abstract: Interaction between 1-[4-(2-carboxyl-ethyl-)phenoxy] phthalocyanine Zinc(II) (ZnPcC1) and albumin (human serum albumin or bovine serum albumin) was studied. ZnPcC1 can be covalently bound to albumin through amide bond formation. The molar ratios of ZnPcC1 to albumins are found to be about 7 : 1 in the covalent bioconjugates. On the other hand, there are strong non-covalent interactions between ZnPcC1 and albumins with a binding constant of ca. 1.0 x 10(5) mol(-1) x L. Binding sites competition experiments suggest that the binding site locates in subdomain I B of human serum albumin. When conjugated to albumin, no matter covalent conjugation or non-covalent conjugation, the ZnPcC1 exhibit more distinctive characteristic monomer absorption than the free ZnPcC1, which is a property beneficial to photodynamic therapy. Covalent conjugation results in the Q-band of ZnPcC1 red-shifting about 5 nm, whereas non-covalent conjugation does not lead to red-shift.
authors.affiliation: College of Chemistry and Chemical Engineering, Fuzhou University, Fuzhou 350108, China. rpxiao8@yahoo.com.cn
authors.forename: Rong-Ping
authors.initials: RP
authors.lastname: Xiao
authors.forename: Na
authors.initials: N
authors.lastname: Zhang
authors.forename: Jian-Dong
authors.initials: JD
authors.lastname: Huang
authors.forename: Han-Hui
authors.initials: HH
authors.lastname: Zhang
mesh_terms: D000418:Albumins / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D006801:Humans; D007211:Indoles / Q000737:chemistry*; D054833:Isoindoles; D009942:Organometallic Compounds / Q000737:chemistry*; D012710:Serum Albumin, Bovine; D013057:Spectrum Analysis; D017967:Zinc Compounds
chemical_list: D000418:Albumins; D007211:Indoles; D054833:Isoindoles; D009942:Organometallic Compounds; D017967:Zinc Compounds; C052159:Zn(II)-phthalocyanine; D012710:Serum Albumin, Bovine