The University of Oxford has made a significant breakthrough in the field of protein analysis with the development of an innovative nanopore technology.
This technology has the capability to identify structural modifications at the single-molecule level, even within complex and lengthy protein chains.
The potential implications of this new protein characterisation technique are significant. It could seamlessly integrate into existing portable nanopore sequencing devices, enabling researchers to rapidly construct inventories of proteins within individual cells and tissues.
This advancement could have practical applications in point-of-care diagnostics, allowing for personalised identification of specific protein variants linked to conditions such as cancer and neurodegenerative disorders.
The team has successfully demonstrated the efficacy of this method in identifying three distinct types of PTM modifications (phosphorylation, glutathionylation, and glycosylation) at the single-molecule level. Remarkably, this method doesn't necessitate the use of labelling agents, enzymes, or additional reagents.
In the realm of cellular biology, it's known that human cells possess around 20,000 genes responsible for encoding proteins. However, the actual number of distinct proteins observed within cells is far higher, reaching over a million different structural variations.
These modified protein variants play crucial roles in biological processes by precisely regulating intricate activities within individual cells. Unravelling the intricate landscape of these variations could lead to a revolutionary understanding of cellular functions. But until now, the challenge of comprehensively cataloguing proteins has remained elusive.
Addressing this challenge, a research team led by scientists at the University of Oxford has devised a method for protein analysis that capitalises on nanopore-based sensing technology.
