Nanopore-Based Protein Identification

被引:95
作者
Bakshloo, Mazdak Afshar [1 ]
Kasianowicz, John J.
Pastoriza-Gallego, Manuela [1 ]
Mathe, Jerome [2 ]
Daniel, Regis [2 ]
Piguet, Fabien [1 ]
Oukhaled, Abdelghani [1 ]
机构
[1] CY Cergy Paris Univ, CNRS, LAMBE, F-95000 Cergy, France
[2] Univ Evry, Univ Paris Saclay, CNRS, LAMBE, F-91000 Evry, France
关键词
MOLECULE MASS-SPECTROMETRY; AMINO-ACIDS; SINGLE; DISCRIMINATION; RESOLUTION; TRANSPORT; AEROLYSIN; NUMBER; DNA; ELECTROPHORESIS;
D O I
10.1021/jacs.1c11758
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The implementation of a reliable, rapid, inexpensive, and simple method for whole-proteome identification would greatly benefit cell biology research and clinical medicine. Proteins are currently identified by cleaving them with proteases, detecting the polypeptide fragments with mass spectrometry, and mapping the latter to sequences in genomic/proteomic databases. Here, we demonstrate that the polypeptide fragments can instead be detected and classified at the single-molecule limit using a nanometer-scale pore formed by the protein aerolysin. Specifically, three different water-soluble proteins treated with the same protease, trypsin, produce different polypeptide fragments defined by the degree by which the latter reduce the nanopore's ionic current. The fragments identified with the aerolysin nanopore are consistent with the predicted fragments that trypsin could produce.
引用
收藏
页码:2716 / 2725
页数:10
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