Effect of Cationic and Anionic Porphyrins on the Structure and Activity of Adenosine Deaminase

Bulletin of the Korean chemical society

Samaneh Hajipour¹  Ali Akbar Saboury¹  Saeed Zakavi¹  Davood Ajloo¹ 

关键词: Porphyrin;    Binding constant;    Fluorescence;    Circular dichroism;    Inhibition constant;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

Kinetic and structural studies have been carried out on the effects of meso-tetrakis(4-sulfonatophenyl)- porphyrin (H2TPPS4) as an anionic and meso-tetrakis(3-N-methyl-pyridyl)porphyrin (H2TMPYP) as a cationic porphyrin with adenosine deaminase (ADA) in 25 mM citrate/phosphate buffer, pH = 4-8, at 37 oC using UVvis spectrophotometry, circular dichroism (CD), fluorescence spectrophotometry as well as molecular dynamics (MD) and molecular docking. Kinetic results showed that the two porphyrins are non-competitive inhibitors. Increasing pH, increases KI and cationic porphyrin has a higher KI and lower binding constant (Kb) at all pH ranges. Analyzing the secondary structure revealed that both ligands decrease the secondary structure and that the anionic porphyrin is more effective.

【 授权许可】

Unknown