热分析法揭示β2-微球蛋白多态性淀粉样生成的能量景观。
Energy landscape of polymorphic amyloid generation of β2-microglobulin revealed by calorimetry.
机构信息
Institute for Protein research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan.
出版信息
Chem Commun (Camb). 2018 Jul 12;54(57):7995-7998. doi: 10.1039/c8cc02718h.
PMID:29967909
Abstract
Understanding of amyloid aggregation in terms of thermodynamics and kinetics is still limited. We herein examined the mechanism of β2-microglobulin amyloidogenesis using our unique method of isothermal titration calorimetry-based thermodynamic/kinetic measurements, and revealed the energy landscape of polymorphic amyloidogenesis under biological environment-mimicking conditions including shear forces and crowding effects.
摘要
尽管人们对淀粉样蛋白聚集的热力学和动力学理解仍有限，但我们通过使用等温滴定量热法（ITC）进行热力学/动力学测量的独特方法，研究了β2-微球蛋白淀粉样蛋白形成的机制，并揭示了在模拟生物环境的条件下，包括剪切力和拥挤效应下，多晶型淀粉样蛋白形成的能量景观。
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