Introduction to nanopore sensing
- Biological nanopores
- Solid state nanopores
The GridION™ system
The MinION™ device: a miniaturised sensing system
Analytes and Applications: DNA, RNA, proteins
Fields of use
The concept of using a nanopore as a biosensor was first proposed in the mid 1990s when nanopores were starting to be researched at academic institutions such as Oxford, Harvard and UCSC - all Oxford Nanopore collaborators. In an industrial setting, Oxford Nanopore was founded in 2005 to translate nanopore science into an electronics-based technology. The end-to-end system includes sample preparation, molecular analysis and informatics, and is designed to provide disruptive user benefits in a number of applications.
Oxford Nanopore has a broad intellectual property portfolio that includes internal innovation and collaborations with world leading nanopore researchers. This IP includes fundamental nanopore sensing techniques through to solid-state nanopore sensing technology including graphene.
A nanopore is, essentially, a nano-scale hole. This hole may be:
• Biological: formed by a pore-forming protein in a membrane such as a lipid bilayer
• Solid-state: formed in synthetic materials such as silicon nitride or graphene
• Hybrid: formed by a pore-forming protein set in synthetic material
A nanopore may be used to identify a target analyte as follows.
This diagram shows a protein nanopore set in an electrically resistant membrane bilayer. An ionic current is passed through the nanopore by setting a voltage across this membrane.
If an analyte passes through the pore or near its aperture, this event creates a characteristic disruption in current. By measuring that current, it is possible to identify the molecule in question. For example, this system can be used to distinguish between the four standard DNA bases G, A, T and C, and also modified bases. It can be used to identify target proteins, small molecules, or to gain rich molecular information, for example to distinguish the enantiomers of ibuprofen or molecular binding dynamics.