AI Article Synopsis
- * The review highlights recent advancements in analytical techniques for studying As-binding proteomes, covering methods like chromatographic separation, biotin-streptavidin probes, and novel fluorescent imaging.
- * The article emphasizes the importance of developing sensitive and high-throughput methods to better understand the molecular mechanisms of arsenic's harmful health effects, suggesting future directions for research in this area.
Article Abstract
Arsenic (As) is one of the most concerning elements due to its high exposure risks to organisms and ecosystems. The interaction between arsenicals and proteins plays a pivotal role in inducing their biological effects on living systems, e.g., arsenicosis. In this review article, the recent advances in analytical techniques and methods of As-binding proteomes were well summarized and discussed, including chromatographic separation and purification, biotin-streptavidin pull-down probes, in situ imaging using novel fluorescent probes, and protein identification. These analytical technologies could provide a growing body of knowledge regarding the composition, level, and distribution of As-binding proteomes in both cells and biological samples, even at the organellar level. The perspectives on analysis of As-binding proteomes are also proposed, e.g., isolation and identification of minor proteins, in vivo targeted protein degradation (TPD) technologies, and spatial As-binding proteomics. The application and development of sensitive, accurate, and high-throughput methodologies of As-binding proteomics would enable us to address the key molecular mechanisms underlying the adverse health effects of arsenicals.
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| http://dx.doi.org/10.1007/s00216-023-04812-6 | DOI Listing |
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