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2016 ; 26
(27
): 4830-4838
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Graphene Nanopores for Protein Sequencing
#MMPMID27746710
Wilson J
; Sloman L
; He Z
; Aksimentiev A
Adv Funct Mater
2016[Jul]; 26
(27
): 4830-4838
PMID27746710
show ga
An inexpensive, reliable method for protein sequencing is essential to unraveling
the biological mechanisms governing cellular behavior and disease. Current
protein sequencing methods suffer from limitations associated with the size of
proteins that can be sequenced, the time, and the cost of the sequencing
procedures. Here, we report the results of all-atom molecular dynamics
simulations that investigated the feasibility of using graphene nanopores for
protein sequencing. We focus our study on the biologically significant
phenylalanine-glycine repeat peptides (FG-nups)-parts of the nuclear pore
transport machinery. Surprisingly, we found FG-nups to behave similarly to single
stranded DNA: the peptides adhere to graphene and exhibit step-wise translocation
when subject to a transmembrane bias or a hydrostatic pressure gradient. Reducing
the peptide's charge density or increasing the peptide's hydrophobicity was found
to decrease the translocation speed. Yet, unidirectional and stepwise
translocation driven by a transmembrane bias was observed even when the ratio of
charged to hydrophobic amino acids was as low as 1:8. The nanopore transport of
the peptides was found to produce stepwise modulations of the nanopore ionic
current correlated with the type of amino acids present in the nanopore,
suggesting that protein sequencing by measuring ionic current blockades may be
possible.