How can proteins be reliably detected when they occur only in minute quantities or hide behind subtle chemical modifications?
Prof. Jan C. Behrends takes this question as the starting point for his recent specialist article “Proteinanalytik mit biologischen Nanoporen” – opening the door to a technology with the potential to transform molecular diagnostics. The article appears in issue 8/2025 of the GIT Laboratory Journal.
The characterisation of low-abundance proteins and post-translational modifications continues to pose major challenges for protein analytics. Conventional methods such as mass spectrometry or immunoassays deliver precise data but reach their limits when ultra-high sensitivity, specificity or even real-time measurements are required. This is precisely where nanopore technology comes into play – a technology that is gaining increasing importance.
Biological nanopores, based on pore-forming proteins, can detect individual molecules without the need for labelling. As a protein passes through the pore, it generates characteristic electrical signals from which size, shape and additional properties can be inferred. In this way, even peptide forms of identical mass can be distinguished – and with significantly lower technical effort compared to mass spectrometry.
nanodiag BW is driving this development forward and is using nanopores as “molecular traps” to analyse post-translational modifications or identify sequences. First assays are already being developed, including for the analysis of lysine methylation.
What can this analytical method already achieve today? And why does this technology promise scalable, cost-efficient and decentralised applications – for example in personalised medicine? Answers can be found in the article in the GIT Laboratory Journal. We wish you an enjoyable read!
