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Identification of tagged glycans with a protein nanopore
Structural complexity of glycans derived from the diversities in composition, linage, configuration, and branching considerably complicates structural analysis. Nanopore-based single-molecule sensing offers the potential to elucidate glycan structure and even sequence glycan. However, the small mole...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10050315/ https://www.ncbi.nlm.nih.gov/pubmed/36977665 http://dx.doi.org/10.1038/s41467-023-37348-5 |
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author | Li, Minmin Xiong, Yuting Cao, Yuchen Zhang, Chen Li, Yuting Ning, Hanwen Liu, Fan Zhou, Han Li, Xiaonong Ye, Xianlong Pang, Yue Zhang, Jiaming Liang, Xinmiao Qing, Guangyan |
author_facet | Li, Minmin Xiong, Yuting Cao, Yuchen Zhang, Chen Li, Yuting Ning, Hanwen Liu, Fan Zhou, Han Li, Xiaonong Ye, Xianlong Pang, Yue Zhang, Jiaming Liang, Xinmiao Qing, Guangyan |
author_sort | Li, Minmin |
collection | PubMed |
description | Structural complexity of glycans derived from the diversities in composition, linage, configuration, and branching considerably complicates structural analysis. Nanopore-based single-molecule sensing offers the potential to elucidate glycan structure and even sequence glycan. However, the small molecular size and low charge density of glycans have restricted direct nanopore detection of glycan. Here we show that glycan sensing can be achieved using a wild-type aerolysin nanopore by introducing a facile glycan derivatization strategy. The glycan molecule can induce impressive current blockages when moving through the nanopore after being connected with an aromatic group-containing tag (plus a carrier group for the neutral glycan). The obtained nanopore data permit the identification of glycan regio- and stereoisomers, glycans with variable monosaccharide numbers, and distinct branched glycans, either independently or with the use of machine learning methods. The presented nanopore sensing strategy for glycans paves the way towards nanopore glycan profiling and potentially sequencing. |
format | Online Article Text |
id | pubmed-10050315 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-100503152023-03-30 Identification of tagged glycans with a protein nanopore Li, Minmin Xiong, Yuting Cao, Yuchen Zhang, Chen Li, Yuting Ning, Hanwen Liu, Fan Zhou, Han Li, Xiaonong Ye, Xianlong Pang, Yue Zhang, Jiaming Liang, Xinmiao Qing, Guangyan Nat Commun Article Structural complexity of glycans derived from the diversities in composition, linage, configuration, and branching considerably complicates structural analysis. Nanopore-based single-molecule sensing offers the potential to elucidate glycan structure and even sequence glycan. However, the small molecular size and low charge density of glycans have restricted direct nanopore detection of glycan. Here we show that glycan sensing can be achieved using a wild-type aerolysin nanopore by introducing a facile glycan derivatization strategy. The glycan molecule can induce impressive current blockages when moving through the nanopore after being connected with an aromatic group-containing tag (plus a carrier group for the neutral glycan). The obtained nanopore data permit the identification of glycan regio- and stereoisomers, glycans with variable monosaccharide numbers, and distinct branched glycans, either independently or with the use of machine learning methods. The presented nanopore sensing strategy for glycans paves the way towards nanopore glycan profiling and potentially sequencing. Nature Publishing Group UK 2023-03-28 /pmc/articles/PMC10050315/ /pubmed/36977665 http://dx.doi.org/10.1038/s41467-023-37348-5 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Li, Minmin Xiong, Yuting Cao, Yuchen Zhang, Chen Li, Yuting Ning, Hanwen Liu, Fan Zhou, Han Li, Xiaonong Ye, Xianlong Pang, Yue Zhang, Jiaming Liang, Xinmiao Qing, Guangyan Identification of tagged glycans with a protein nanopore |
title | Identification of tagged glycans with a protein nanopore |
title_full | Identification of tagged glycans with a protein nanopore |
title_fullStr | Identification of tagged glycans with a protein nanopore |
title_full_unstemmed | Identification of tagged glycans with a protein nanopore |
title_short | Identification of tagged glycans with a protein nanopore |
title_sort | identification of tagged glycans with a protein nanopore |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10050315/ https://www.ncbi.nlm.nih.gov/pubmed/36977665 http://dx.doi.org/10.1038/s41467-023-37348-5 |
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