{"title":"Discrimination and Translocation of Charged Proteinogenic Amino Acids through a Single-Walled Carbon Nanotube.","authors":"Yingjun Shen, Mingming Ding","doi":"10.1021/acs.jpcb.4c08692","DOIUrl":null,"url":null,"abstract":"<p><p>Nanopore sensing relies on associating the measured current signals with specific features of the target molecules. The diversity of amino acids presents significant challenges in detecting and sequencing peptides and proteins. The hollow and uniform tubular structure of single-walled carbon nanotubes (SWCNTs) makes them ideal candidates for nanopore sensors. Here, we demonstrate by molecular dynamics simulations the discrimination and translocation of charged proteinogenic amino acids through the nanopore sensor formed by inserting a SWCNT into lipid bilayers. Moreover, our analysis suggests that the current blockade is influenced not only by excluded atomic volume but also by noncovalent interactions between amino acids and SWCNT during similar helical translocation. The presence of noncovalent interactions enhances the understanding of current differences in nanopore translocation of molecules with similar excluded atomic volume. This finding provides new perspectives and applications for the optimal design of SWCNT nanopore sensors.</p>","PeriodicalId":60,"journal":{"name":"The Journal of Physical Chemistry B","volume":" ","pages":"3502-3513"},"PeriodicalIF":2.8000,"publicationDate":"2025-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Journal of Physical Chemistry B","FirstCategoryId":"1","ListUrlMain":"https://doi.org/10.1021/acs.jpcb.4c08692","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/3/25 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
引用次数: 0
Abstract
Nanopore sensing relies on associating the measured current signals with specific features of the target molecules. The diversity of amino acids presents significant challenges in detecting and sequencing peptides and proteins. The hollow and uniform tubular structure of single-walled carbon nanotubes (SWCNTs) makes them ideal candidates for nanopore sensors. Here, we demonstrate by molecular dynamics simulations the discrimination and translocation of charged proteinogenic amino acids through the nanopore sensor formed by inserting a SWCNT into lipid bilayers. Moreover, our analysis suggests that the current blockade is influenced not only by excluded atomic volume but also by noncovalent interactions between amino acids and SWCNT during similar helical translocation. The presence of noncovalent interactions enhances the understanding of current differences in nanopore translocation of molecules with similar excluded atomic volume. This finding provides new perspectives and applications for the optimal design of SWCNT nanopore sensors.
期刊介绍:
An essential criterion for acceptance of research articles in the journal is that they provide new physical insight. Please refer to the New Physical Insights virtual issue on what constitutes new physical insight. Manuscripts that are essentially reporting data or applications of data are, in general, not suitable for publication in JPC B.