Quantification of Protein Glycosylation Using Nanopores

Roderick Corstiaan Abraham Versloot, Florian Leonardus Rudolfus Lucas, Liubov Yakovlieva, Matthijs Jonathan Tadema, Yurui Zhang, Thomas M Wood, Nathaniel I Martin, Siewert J Marrink, Marthe T C Walvoort*, Giovanni Maglia*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

26 Citaten (Scopus)
94 Downloads (Pure)

Samenvatting

Although nanopores can be used for single-molecule sequencing of nucleic acids using low-cost portable devices, the characterization of proteins and their modifications has yet to be established. Here, we show that hydrophilic or glycosylated peptides translocate too quickly across FraC nanopores to be recognized. However, high ionic strengths (i.e., 3 M LiCl) and low pH (i.e., pH 3) together with using a nanopore with a phenylalanine at its constriction allows the recognition of hydrophilic peptides, and to distinguish between mono- and diglycosylated peptides. Using these conditions, we devise a nanopore method to detect, characterize, and quantify post-translational modifications in generic proteins, which is one of the pressing challenges in proteomic analysis.

Originele taal-2English
Artikelnummer2c10338
Pagina's (van-tot)5357-5364
Aantal pagina's8
TijdschriftNano Letters
Volume22
Nummer van het tijdschrift13
Vroegere onlinedatum29-jun.-2022
DOI's
StatusPublished - 13-jul.-2022

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