MoS2 nanopore identifies single amino acids with sub-1 Dalton resolution

The sequencing of single protein molecules using nanopores is faced with a huge challenge due to the lack of resolution needed to resolve single amino acids. Here we report the direct experimental identification of single amino acids in nanopores. With atomically engineered regions of sensitivity co...

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Veröffentlicht in:Nature communications 2023-05, Vol.14 (1), p.2895-2895, Article 2895
Hauptverfasser: Wang, Fushi, Zhao, Chunxiao, Zhao, Pinlong, Chen, Fanfan, Qiao, Dan, Feng, Jiandong
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Sprache:eng
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Zusammenfassung:The sequencing of single protein molecules using nanopores is faced with a huge challenge due to the lack of resolution needed to resolve single amino acids. Here we report the direct experimental identification of single amino acids in nanopores. With atomically engineered regions of sensitivity comparable to the size of single amino acids, MoS 2 nanopores provide a sub-1 Dalton resolution for discriminating the chemical group difference of single amino acids, including recognizing the amino acid isomers. This ultra-confined nanopore system is further used to detect the phosphorylation of individual amino acids, demonstrating its capability for reading post-translational modifications. Our study suggests that a sub-nanometer engineered pore has the potential to be applied in future chemical recognition and de novo protein sequencing at the single-molecule level. Protein sequencing is one of the key aims of the nanopore field. Working toward this goal, here the authors report the direct identification of single amino acids in MoS 2 nanopores with sub-1 Dalton resolution, as well as the discrimination of the amino acid isomers and amino acid phosphorylation.
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-023-38627-x