title: [Study on interaction mechanism between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin and bovine serum albumin by fluorescence method].
abstract: In the present paper, the binding reaction between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin (TPP-Zn) and bovine serum albumin (BSA) was studied at different temperatures by fluorescence method. It was shown that meso-tetra-(4-hydroxyphenyl)-Zn porphyrin has a strong ability of quenching the fluorescence of bovine serum albumin. Based on the mechanisms of fluorescence quenching of bovine serum albumin caused by meso-tetra-(4-hydroxyphenyl)-Zn porphyrin, the binding constants between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin and bovine serum albumin were measured under different temperatures. The experiment showed that meso-tetra-(4-hydroxyphenyl)-Zn porphyrin and bovine serum albumin have strong interactions. The binding constants of the reaction at 27 degrees C, 35 degrees C and 42 degrees C were 1.521 x 10(6) L x mol(-1), 7.048 x 10(5) L x mol(-1) and 1.473 x 10(5) L x mol(-1), respectively, and were decreased with increasing the temperature. The constants of maximum diffusion collision quenching rate-K(q) were above 2.0 x 10(10) L x mol(-1) x s(-1). Therefore, the sort of quenching between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin and bovine serum albumin was determined as static quenching. By the theory of Förster of non-radiation energy transfer, the binding distance and the energy transfer efficiency at 27 degrees C between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin (accepter of energy) and bovine serum albumin (donor of energy) were obtained, respectively. The binding distance was 3.72 nm, which is less than 7 nm, therefore, the interaction was similar to the non-radiation energy transfer, and the static quenching was further proved. According to the thermodynamic parameters, the main sorts of binding force between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin and bovine serum albumin could be judged as electrostatic force when deltaG < 0, deltaH < 0 and deltaS > 0.
authors.affiliation: School of Chemistry and Chemical Engineering, University of Jinan, Ji'nan 250022, China. sdjndxwq@163.com
authors.forename: Li-Na
authors.initials: LN
authors.lastname: Zhang
authors.forename: Xin
authors.initials: X
authors.lastname: Chen
authors.forename: Yang
authors.initials: Y
authors.lastname: Xia
authors.forename: Dan
authors.initials: D
authors.lastname: Wu
authors.forename: Jing-Hua
authors.initials: JH
authors.lastname: Yu
authors.forename: Bin
authors.initials: B
authors.lastname: Du
authors.forename: Qin
authors.initials: Q
authors.lastname: Wei
mesh_terms: D000818:Animals; D002417:Cattle; D007700:Kinetics; D008665:Metalloporphyrins / Q000737:chemistry* / Q000378:metabolism*; D011166:Porphyrins / Q000737:chemistry*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013816:Thermodynamics; D015032:Zinc / Q000737:chemistry*
chemical_list: D008665:Metalloporphyrins; D011166:Porphyrins; C481734:meso-tetra-(4-hydroxyphenyl)porphyrin; D012710:Serum Albumin, Bovine; D015032:Zinc