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通过蛋白质设计克服对金属选择性的普遍限制

Tae Su Choi¹, F Akif Tezcan²

¹Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.

|March 3, 2022

概括

这项研究引入了一种灵活的人造蛋白 (AB2),它克服了天然的金属结合偏好. 它在铜上选择性地结合较少的过渡金属,为金属封存剂提供了新的策略.

科学领域:

蛋白质工程
生物化学
有机生物化学

背景情况:

选择性金属协调对于金属蛋白的功能至关重要,但由于蛋白质的灵活性和有限的氨基酸功能,因此很难实现.
自然蛋白质通常遵循欧文-威廉姆斯系列,优先结合Cu2+和Zn2+而不是其他过渡金属,因此需要复杂的生物系统来实现金属平衡.
现有的金属选择性策略通常依赖于结构预组织,这在动态的生物环境中可能是有限制的.

研究的目的:

在实验室和细胞中设计和描述一种在热力学上克服欧文-威廉姆斯系列限制的人造蛋白质.
证明可以利用蛋白质的灵活性来实现金属选择性,比Cu2+更有利于低欧文-威廉姆斯过渡金属.
探索创建选择性金属封存剂的新设计原则.

主要方法:

一种灵活的人工二元蛋白的设计, (AB) 2.
在体外和细胞内实验以评估金属结合亲和性和选择性.
结构分析以了解金属依赖的形状变化和协调几何学.

主要成果:

人工二元蛋白 (AB) 2在热力学上有利于低欧文-威廉姆斯过渡金属与Cu2+的结合.
蛋白质的灵活性使 (AB) 2能够采用不同的金属依赖形状.
由于不良的几何形状,发现了结构合的协调部位,不利于Cu2+结合.

结论:

灵活性是实现人工蛋白质金属选择性的有价值的设计元素.
(AB) 2为克服固有的金属结合偏好提供了一个新的例子.
该研究提供了用于各种应用的选择性金属封存剂的设计原则.

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