Real-time shape approximation and fingerprinting of single proteins using a nanopore.

Autor: Yusko EC; Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA., Bruhn BR; Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA., Eggenberger OM; Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA.; Adolphe Merkle Institute, University of Fribourg, Chemin des Verdiers 4, CH-1700 Fribourg, Switzerland., Houghtaling J; Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA.; Adolphe Merkle Institute, University of Fribourg, Chemin des Verdiers 4, CH-1700 Fribourg, Switzerland., Rollings RC; Department of Physics, University of Arkansas, Fayetteville, Arkansas 72701, USA., Walsh NC; Department of Physics, University of Arkansas, Fayetteville, Arkansas 72701, USA., Nandivada S; Department of Physics, University of Arkansas, Fayetteville, Arkansas 72701, USA., Pindrus M; Department of Pharmaceutical Sciences, University of Connecticut, Storrs, Connecticut 06269, USA., Hall AR; Department of Biomedical Engineering and Comprehensive Cancer Center, Wake Forest University School of Medicine, Winston Salem, North Carolina 27157, USA., Sept D; Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA.; Center for Computational Medicine and Biology, University of Michigan, Ann Arbor, Michigan 48109, USA., Li J; Department of Physics, University of Arkansas, Fayetteville, Arkansas 72701, USA., Kalonia DS; Department of Pharmaceutical Sciences, University of Connecticut, Storrs, Connecticut 06269, USA., Mayer M; Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA.; Adolphe Merkle Institute, University of Fribourg, Chemin des Verdiers 4, CH-1700 Fribourg, Switzerland.; Biophysics Program, University of Michigan, Ann Arbor, Michigan 48109, USA.
Jazyk: angličtina
Zdroj: Nature nanotechnology [Nat Nanotechnol] 2017 May; Vol. 12 (4), pp. 360-367. Date of Electronic Publication: 2016 Dec 19.
DOI: 10.1038/nnano.2016.267
Abstrakt: Established methods for characterizing proteins typically require physical or chemical modification steps or cannot be used to examine individual molecules in solution. Ionic current measurements through electrolyte-filled nanopores can characterize single native proteins in an aqueous environment, but currently offer only limited capabilities. Here we show that the zeptolitre sensing volume of bilayer-coated solid-state nanopores can be used to determine the approximate shape, volume, charge, rotational diffusion coefficient and dipole moment of individual proteins. To do this, we developed a theory for the quantitative understanding of modulations in ionic current that arise from the rotational dynamics of single proteins as they move through the electric field inside the nanopore. The approach allows us to measure the five parameters simultaneously, and we show that they can be used to identify, characterize and quantify proteins and protein complexes with potential implications for structural biology, proteomics, biomarker detection and routine protein analysis.
Databáze: MEDLINE
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