吸附在石墨烯上的芘-丁酸连接的蛋白质分子的可能双稳态结构：理论研究
Possible bi-stable structures of pyrene-butanoic-acid-linked protein molecules adsorbed on graphene: Theoretical study
AI总结：
本研究通过理论分析发现，经PASE连接剂固定在石墨烯上的蛋白质因连接剂的空间位阻效应存在双稳态构象及活化能垒型能量面，为振荡器型生物传感器灵敏度提升提供指导。
摘要：
我们从理论上分析了通过1-芘丁酸琥珀酰亚胺酯（PASE）连接剂固定在石墨烯上的蛋白质分子的多种可能构象。研究证实，PASE呈现的两种双稳态构象之间的活化能垒源于该分子中芘基团上的一个氢与烷基基团上的一个氢之间的空间位阻效应。即使在结合蛋白质后，只要由烷基和芘基组成的连接剂局部结构得以保持，这种空间位阻效应依然存在。因此，通过单个PASE连接剂固定的蛋白质，其动力学行为很可能在石墨烯上的双稳态构象之间呈现出活化能垒型能量面。我们讨论了这类能量面出现时可预期的蛋白质传感器，并提出了提升灵敏度的指导方针，尤其是作为振荡器型生物传感器的应用方向。
英文摘要：
We theoretically analyze possible multiple conformations of protein molecules immobilized by 1-pyrenebutanoic-acid-succinimidyl-ester (PASE) linkers on graphene. The activation barrier between two bi-stable conformations exhibited by PASE is confirmed to be based on the steric hindrance effect between a hydrogen on the pyrene group and a hydrogen on the alkyl group of this molecule. Even after the protein is supplemented, this steric hindrance effect remains if the local structure of the linker consisting of an alkyl group and a pyrene group is maintained. Therefore, it is likely that the kinetic behavior of a protein immobilized with a single PASE linker exhibits an activation barrier-type energy surface between the bi-stable conformations on graphene. We discuss the expected protein sensors when this type of energy surface appears and provide a guideline for improving the sensitivity, especially as an oscillator-type biosensor.
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