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THE INVESTIGATION ON THE SELF-ASSEMBLY DRIVING FORCE OF HBV CAPSID PROTEIN

Liu, Qiao, Liu
http://rave.ohiolink.edu/etdc/view?acc_num=akron152233306275171

Abstract Details

2018, Master of Science, University of Akron, Polymer Science.
Hepatitis B virus (HBV) icosahedral capsids can be assembled from tens of dimer proteins in the presence of some monovalent or divalent salt in vitro. The capsids, which have two different morphologies: T=3 or T=4, can be characterized by TEM and fractionated by using sucrose gradient. To study the charge effects in capsid assembly process, two charged amino acid residues on wild type(WT) dimer protein are mutated and get a mutant dimer called D2ND4N(D/N). Then Assembly kinetics and thermodynamics of these two dimers were studied. We found that the concentration of protein, pH, ionic strength, all of these factors have impact on the self-assembly behavior of HBV virus capsid. According to experimental results and analysis, the electrostatic force is confirmed to play a critical role in governing the self-assembly of HBV virus capsid. Meanwhile the ionic strength in the nucleating stage of virus capsid assembly was found to have a great influence on dimorphism of virus capsid. This phenomenon is explained by the narrowing of energy barrier difference for T=4 and T=3 capsids. Compared with hydrophilic macroions, the presence of hydrophobic domains is the major characteristic in charged protein dimer. And the presence of the short ranged hydrophobic interactions explains the absence of the self-recognition behavior between WT and D2ND4N dimer in experiment. Temperature also impacts on formation and dissociation of the virus capsid assembly via influence the hydrophobic interaction among protein subunits. High temperature facilitates the self-assembly while low temperature refrains the formation of virus capsid. Exploring the driving force and its controlling means during HBV virus capsid assembly is beneficial in prevention of HBV virus induced disease and development of antivirus drug in the future.
Tianbo Liu (Advisor)
Toshikazu Miyoshi (Committee Member)
49 p.
Biology; Biophysics; Physical Chemistry
Self-assembly, HBV virus capsid, Electrostatic interaction, Hydrophobic interaction

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Citations

  • Liu, Liu, Q. (2018). THE INVESTIGATION ON THE SELF-ASSEMBLY DRIVING FORCE OF HBV CAPSID PROTEIN [Master's thesis, University of Akron]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=akron152233306275171

    APA Style (7th edition)

  • Liu, Liu, Qiao. THE INVESTIGATION ON THE SELF-ASSEMBLY DRIVING FORCE OF HBV CAPSID PROTEIN . 2018. University of Akron, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=akron152233306275171.

    MLA Style (8th edition)

  • Liu, Liu, Qiao. "THE INVESTIGATION ON THE SELF-ASSEMBLY DRIVING FORCE OF HBV CAPSID PROTEIN ." Master's thesis, University of Akron, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=akron152233306275171

    Chicago Manual of Style (17th edition)

akron152233306275171
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© 2018, some rights reserved.Creative Commons License THE INVESTIGATION ON THE SELF-ASSEMBLY DRIVING FORCE OF HBV CAPSID PROTEIN by Qiao Liu Liu is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. Based on a work at etd.ohiolink.edu.
This open access ETD is published by University of Akron and OhioLINK.