Resolving Chemical Modifications to a Single Amino Acid within a Peptide Using a Biological Nanopore.

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ID: 47754
2019
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Abstract
While DNA sequencing is now amply available, fast, and inexpensive, protein sequencing remains a tremendous challenge. Nanopores may allow for developing a protein sequencer with single-molecule capabilities. As identification of 20 different amino acids currently presents an unsurmountable challenge, fingerprinting schemes are pursued, in which only a subset of amino acids is labeled and detected. This requires modification of amino acids with chemical structures that generate a distinct nanopore ionic current signal. Here, we use a model peptide and the fragaceatoxin C nanopore to characterize six potential tags for a fingerprinting approach using nanopores. We find that labeled and unlabeled proteins can be clearly distinguished and that sensitive detection is obtained for labels with a spectrum of different physicochemical properties such as mass (427-1275 Da), geometry, charge, and hydrophobicity. Additionally, information about the position of the label along the peptide chain can be obtained from individual current-blockade event features. The results represent an important advance toward the development of a single-molecule protein-fingerprinting device with nanopores.
Reference Key
restrepoprez2019resolvingacs Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Restrepo-Pérez, Laura;Huang, Gang;Bohländer, Peggy R;Worp, Nathalie;Eelkema, Rienk;Maglia, Giovanni;Joo, Chirlmin;Dekker, Cees;
Journal acs nano
Year 2019
DOI
10.1021/acsnano.9b05156
URL
Keywords
amino acid labeling biological nanopores nanopore protein analysis protein fingerprinting single-molecule protein sequencing

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