Kinetics versus Thermodynamics in Virus Capsid Polymorphism
Kinetics versus Thermodynamics in Virus Capsid Polymorphism
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DOI：
10.1021/acs.jpcb.6b01953
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发表时间：
2016-07-07
影响因子：
3.3
通讯作者：
Kegel, Willem
中科院分区：
文献类型：
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作者：
Moerman, Pepijn;van der Schoot, Paul;Kegel, Willem
在适当的物理化学条件下，病毒外壳蛋白在水溶液中自发自组装成空壳，其驱动力为每个键的相互作用自由能，约为热能 k(B)T 的 2-5 倍。对于这种看似适度的相互作用强度，每个蛋白质构建块仍然获得非常大的结合自由能，在 10 到 20 k(B)T 之间。正因为如此，关于组装过程是可逆还是不可逆存在争议。在这里，我们从成核理论和质量作用热力学的角度讨论体外实验中观察到的衣壳多态性。我们特别考虑曲率自由能项对蛋白质之间有效相互作用势的潜在贡献。从这些模型中，我们提出实验可能最终揭示病毒衣壳组装成多晶型物混合物是可逆还是不可逆过程。
Virus coat proteins spontaneously self-assemble into empty shells in aqueous solution under the appropriate physicochemical conditions, driven by an interaction free energy per bond on the order of 2-5 times the thermal energy k(B)T. For this seemingly modest interaction strength, each protein building block nonetheless gains a very large binding free energy, between 10 and 20 k(B)T. Because of this, there is debate about whether the assembly process is reversible or irreversible. Here we discuss capsid polymorphism observed in in vitro experiments from the perspective of nucleation theory and of the thermodynamics of mass action. We specifically consider the potential contribution of a curvature free energy term to the effective interaction potential between the proteins. From these models, we propose experiments that may conclusively reveal whether virus capsid assembly into a mixture of polymorphs is a reversible or an irreversible process.