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Trypsin Binding with Copper Ions Scavenges Superoxide: Molecular Dynamics-Based Mechanism Investigation

Author

Listed:
  • Xin Li

    (College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471023, China
    Ministry of Education Key Laboratory of Cell Activities and Stress Adaptations, Lanzhou University, Lanzhou 730000, China)

  • Yongliang Zhong

    (College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471023, China)

  • Chunyan Zhao

    (School of Pharmacy, Lanzhou University, Lanzhou 730000, China)

Abstract

Trypsin is a serine protease, which has been proved to be a novel superoxide scavenger. The burst of superoxide induced by polychlorinated biphenyls can be impeded by trypsin in both wild type and sod knockout mutants of Escherichia coli . The experimental results demonstrated that the activities of superoxide scavenging of trypsin were significantly accelerated by Cu ions. Also, with the addition of Cu ions, a new β-sheet (β7) transited from a random coil in the Cu(II)-trypsin (TP) system, which was favorable for the formation of more contacts with other sheets of trypsin. Residue–residue network analysis and the porcupine plots proved that the Cu ion in trypsin strengthened some native interactions among residues, which ultimately resulted in much greater stability of the Cu(II)-TP system. Moreover, compact and stable trypsin structures with Cu ions might be responsible for significantly provoking the activity of superoxide scavenging.

Suggested Citation

  • Xin Li & Yongliang Zhong & Chunyan Zhao, 2018. "Trypsin Binding with Copper Ions Scavenges Superoxide: Molecular Dynamics-Based Mechanism Investigation," IJERPH, MDPI, vol. 15(1), pages 1-13, January.
    • Handle: RePEc:gam:jijerp:v:15:y:2018:i:1:p:139-:d:127063
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