Journal
ACS NANO
Volume 9, Issue 2, Pages 1089-1098Publisher
AMER CHEMICAL SOC
DOI: 10.1021/nn506606e
Keywords
nanopore; protein sensor; single-molecule detection; OmpG
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Funding
- University of Massachusetts as part of the Chemistry-Biology Interface training grant [T32 GM08515]
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Oligomeric protein nanopores with rigid structures have been engineered for the purpose of sensing a wide range of analytes including small molecules and biological species such as proteins and DNA. We chose a monomeric beta-barrel porin, OmpG, as the platform from which to derive the nanopore sensor. OmpG is decorated with seven flexible loops that move dynamically to create a distinct gating pattern when ionic current passes through the pore. Biotin was chemically tethered to the most flexible one of these loops. The gating characteristic of the loops movement in and out of the porin was substantially altered by analyte protein binding. The gating characteristics of the pore with bound targets were remarkably sensitive to molecular identity, even providing the ability to distinguish between homologues within an antibody mixture. A total of five gating parameters were analyzed for each analyte to create a unique fingerprint for each biotin-binding protein. Our exploitation of gating noise as a molecular identifier may allow more sophisticated sensor design, while OmpGs monomeric structure greatly simplifies nanopore production
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