Label-free high-precise nanopore detection of endopeptidase activity of anthrax lethal factor regulated by diverse conditions

Li, Ming-Han; Chen, Shanchuan; Wang, Yunjiao; Zhang, Shaoxia; Song, Dandan; Tian, Rong; Geng, Jia; Wang, Liang

doi:10.1016/j.bios.2022.114800

Cited by 2 publications

(1 citation statement)

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“…Besides, relying on the ionic transport, nanopore electro measurement not only exhibits excellent performance for protein profiling, [ 20‐22 ] but also offers opportunities to illustrate phenomena of protein conformational changes, [ 23 ] protein‐protein interaction, [ 24‐25 ] and explore enzyme dynamics in real‐time manner. [ 26‐27 ] Interestingly, nanopore is also possible at this stage, to directly identify the detailed sequence changes taking place during a biosynthesis of a protein, by enzymatic modifications (post‐translational modifications), [ 28‐29 ] and decoding (sequencing). [ 30‐32 ] Therefore, we postulate that nanopore would be an important contribution to carbonic anhydrase measurement, by precise analysis at the single‐ molecule level.…”

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confidence: 99%

Single‐Molecule Measurement of Carbonic Anhydrase in Cation Coordinated Environment Using MspA Nanopore^†

et al. 2023

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Comprehensive Summary Carbonic anhydrase accounts for catalytic reaction of CO2/HCO3– transformation, thus resulting in neutralization and acidification of the cellular environment, thereby favoring tumor development. Hence, it is a classical protein model of greatly biocatalytic significance as well as a highly expressed biomarker with renal tumor. We herein proposed a single‐molecule measurement on carbonic anhydrase using MspA nanopore, in [BMIM+] and asymmetric K+/Ca2+ cationic coordinated environment, instead of usual symmetric KCl/NaCl electrolyte. Significantly, our empirical analysis showed that asymmetric K+/Ca2+ cationic environment contributes to distinguishable current modulations, thus yielding better resolution for carbonic anhydrase measurement, which is independent of applied voltage and more importantly, is stable enough at varied pH conditions and for very low concentration test in urine sample. Our results provide a classical model for nanopore protein analysis, and may also permit biocatalytic measurement at single‐molecule level.

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Section: Background and Originality Contentmentioning

confidence: 99%

Single‐Molecule Measurement of Carbonic Anhydrase in Cation Coordinated Environment Using MspA Nanopore^†

et al. 2023

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Protein nanopore-based sensors for public health analyte detection

Zhang,

Hu,

Liu

et al. 2024

J. Mater. Chem. B

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Label-free high-precise nanopore detection of endopeptidase activity of anthrax lethal factor regulated by diverse conditions

Cited by 2 publications

References 34 publications

Single‐Molecule Measurement of Carbonic Anhydrase in Cation Coordinated Environment Using MspA Nanopore^†

Single‐Molecule Measurement of Carbonic Anhydrase in Cation Coordinated Environment Using MspA Nanopore^†

Protein nanopore-based sensors for public health analyte detection

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Label-free high-precise nanopore detection of endopeptidase activity of anthrax lethal factor regulated by diverse conditions

Cited by 2 publications

References 34 publications

Single‐Molecule Measurement of Carbonic Anhydrase in Cation Coordinated Environment Using MspA Nanopore†

Single‐Molecule Measurement of Carbonic Anhydrase in Cation Coordinated Environment Using MspA Nanopore†

Protein nanopore-based sensors for public health analyte detection

Contact Info

Product

Resources

About

Single‐Molecule Measurement of Carbonic Anhydrase in Cation Coordinated Environment Using MspA Nanopore^†

Single‐Molecule Measurement of Carbonic Anhydrase in Cation Coordinated Environment Using MspA Nanopore^†