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

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

SUBMITTER: Restrepo-Perez L 

PROVIDER: S-EPMC6933820 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature