Chemical Research in Chinese Universities ›› 2020, Vol. 36 ›› Issue (2): 247-253.doi: 10.1007/s40242-020-0018-1

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Effects of Molecular Crowding on G-Quadruplex-hemin Mediated Peroxidase Activity

LIU Lu1, LIN Jingfang1, SONG Yanling1, YANG Chaoyong1,2, ZHU Zhi1   

  1. 1. Key Laboratory of Spectrochemical Analysis&Instrumentation, Ministry of Education, Key Laboratory of Chemical Biology of Fujian Province, State Key Laboratory of Physical Chemistry of Solid Surfaces, Collaborative Innovation Center of Chemistry for Energy Materials, Department of Chemical Engineering, Department of Chemical Biology, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, P. R. China;
    2. Institute of Molecular Medicine, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 200127, P. R. China
  • Received:2020-01-28 Revised:2020-02-27 Online:2020-04-01 Published:2020-03-02
  • Contact: ZHU Zhi E-mail:zhuzhi@xmu.edu.cn
  • Supported by:
    Supported by the National Natural Science Foundation of China(Nos.21775128, 21435004, 21735004, 21705024 and 21521004) and the Program for Changjiang Scholars and Innovative Research Team in University, China(No.IRT13036).

Abstract: The concentration of macromolecules in cells can reach up to 50-400 mg/mL. They occupy 40%(volume fraction) of the whole cellar space, known as molecular crowding. The diluted solution condition in vitro is different from the crowded physiological condition in vivo. Therefore, the simulation of the physiological condition is necessary for obtaining the reliable results. It has been reported that G-quadruplex can bind to hemin to enhance its catalytic function for generating oxygen radicals, which can oxidize the lipids, proteins and DNA, thus leading to the damage of cells and tissues. In this paper, we chose PEG400 as molecular crowding reagent to simulate the molecular crowding environment in vivo. The catalytic characteristics of G-quadruplex-hemin complex in H2O2-ABTS system have been investigated[ABTS=2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate)]. The results showed that the binding affinity of G-quadruplex and hemin was decreased with the increasing of PEG400 concentration. They even lose their binding affinity in the presence of 40% PEG400. As a result, the peroxidase activity of G-quadruplex-hemin also reduced. Therefore, in physiological condition, hemin might not bind to G-quadruplex and it might not be the main reason to cause the damages of cells and tissues.

Key words: G-Quadruplex, Hemin, Molecular crowding, Peroxidase activity