Insights into protein sequencing with an α-Hemolysin nanopore by atomistic simulations.

ABSTRACT: Single molecule protein sequencing would represent a disruptive burst in proteomic research with important biomedical impacts. Due to their success in DNA sequencing, nanopore based devices have been recently proposed as possible tools for the sequencing of peptide chains. One of the open questions in nanopore protein sequencing concerns the ability of such devices to provide different signals for all the 20 standard amino acids. Here, using equilibrium all-atom molecular dynamics simulations, we estimated the pore clogging in α-Hemolysin nanopore associated to 20 different homopeptides, one for each standard amino acid. Our results show that pore clogging is affected by amino acid volume, hydrophobicity and net charge. The equilibrium estimations are also supported by non-equilibrium runs

SUBMITTER: Di Muccio G 

PROVIDER: S-EPMC6478933 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature