A highly sensitive nanopore platform for measuring RNase A activity.
Autor: | Zheng H; Department of Chemistry, University of Missouri, Columbia, MO 65211, USA., Munusamy S; Department of Chemistry, University of Missouri, Columbia, MO 65211, USA., Arora P; Department of Chemistry, Illinois Institute of Technology, Chicago, IL, 60616, USA., Jahani R; Department of Chemistry, University of Missouri, Columbia, MO 65211, USA., Guan X; Department of Chemistry, University of Missouri, Columbia, MO 65211, USA. Electronic address: xgpc2@missouri.edu. |
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Jazyk: | angličtina |
Zdroj: | Talanta [Talanta] 2024 Aug 15; Vol. 276, pp. 126276. Date of Electronic Publication: 2024 May 22. |
DOI: | 10.1016/j.talanta.2024.126276 |
Abstrakt: | Ribonuclease A (RNase A) plays significant roles in several physiological and pathological conditions and can be used as a valuable diagnostic biomarker for human diseases such as myocardial infarction and cancer. Hence, it is of great importance to develop a rapid and cost-effective method for the highly sensitive detection of RNase A. The significance of RNase A assay is further enhanced by the growing attention from the biotechnology and pharmaceutical industries to develop RNA-based vaccines and drugs in large part as a result of the successful development of mRNA vaccines in the COVID-19 pandemic. Herein, we report a label-free method for the detection of RNase A by monitoring its proteolytic cleavage of an RNA substrate in a nanopore. The method is ultra-sensitive with the limit of detection reaching as low as 30 fg per milliliter. Furthermore, sensor selectivity and the effects of temperature, incubation time, metal ion, salt concentration on sensor sensitivity were also investigated. Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (Copyright © 2024 Elsevier B.V. All rights reserved.) |
Databáze: | MEDLINE |
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