Revealing Protein Binding Affinity on Metal Surfaces:An Electrochemistry Approach
Revealing Protein Binding Affinity on Metal Surfaces:An Electrochemistry Approach
复制标题
揭示金属表面上的蛋白质结合亲和力：电化学方法
DOI：
10.1039/d1cc07098c
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发表时间：
2022
影响因子：
4.9
通讯作者：
Bin Ren
中科院分区：
文献类型：
--
作者：
Danya Lyu;Pingshi Wang;Shuo zhang;Guokun Liu;Bin Ren
揭示病毒与环境基质表面之间的结合亲和力对于评估固定化病毒的生物活性和伴随的与病毒相关的间接感染途径至关重要。对于SARS-CoV-2在不锈钢上持续感染几天，而在铜上只有几个小时的理解仍不清楚。用电化学计时电流法研究了SARS-CoV-2在金属表面的亲和力。SARS-CoV-2的替代物SRBD在金表面的吸附容量最大，其次是铜，在不锈钢表面的吸附容量最低。SRBD与铜的强结合是在环境条件下自然生长的Cu2O的结果。电化学电容的测量为通过导电环境基质探索和评估间接病毒相关感染途径的潜在风险提供了一种简单的策略。
Revealing the binding affinity between viruses and surfaces of environmental matrices is crucial to evaluate the bioactivity of an immobilized virus and accompanying indirect virus-related infection pathways. The understanding for SARS-CoV-2 remaining infective for even days on stainless steel but only hours on copper is still unclear. Electrochemical chronoamperometry, ultrasensitive to interfacial capacitance on surface species, was used to investigate the binding affinity of SARS-CoV-2 on metal surfaces. SRBD, the surrogate of SARS-CoV-2, shows the highest adsorption capacity on a gold surface, followed by Cu, but lowest on a stainless steel surface. The strong binding of SRBD on copper is a result of the naturally grown Cu2O under ambient conditions. Measurement of electrochemical capacitance provides a simple strategy to explore and evaluate the potential risk of an indirect virus-related infection pathway through conductive environmental matrices.