Joan van der Waals colloquium
- 26 oktober 2018
- Drinks afterwards (17.00h)
Niels Bohrweg 2
2333 CA Leiden
- De Sitterzaal
Nanopore bio-sensing: past, present and future
Nanopores are single-molecule biosensors capable of concentrating and sensing a wide-spectrum of electrically-charged biomolecules, including nucleic acids and proteins. In a nanopore system, an electrical field pulls the electrically-charged analyte towards and through a nanometer-scale pore. When a biomolecule enters the nanopore, it partially blocks the ion current flowing through the nanopore, creating a time-dependent current trace, used to characterize the biomolecule’s properties. This simple concept underlies nanopore DNA sequencing, which has been recently commercialized and achieved worldwide success after more than two decades of research. Most studies to date involved Ohmic electrical sensing (conductance) as a mean to detect and characterize the translocation of bioanalytes through the pore. However, in many cases the addition of an independent optical sensing, can substantially enhance the method’s scope of potential biomedical applications. To that end our lab has been developing ultra-sensitive opto-electrical nanopore tools and biosensors (“optipores”) for a variety of applications.
In this lecture I will review the fundamental principles governing biomolecule capture and sensing by nanopores. Then I will discuss some of the latest advancements in the optipore field: First, the ability to rapidly form on demand nanopores in thin SiNx using a feedback-controlled optical etching. Second, using light to modulate the translocation speed of DNAs and proteins in real-time. Third, combing single-molecule fluorescence sensing simultaneously with the Ohmic electrical sensing for single-molecule DNA methylation quantification using a single-step labeling reaction and optipore devices, as well as DNA barcode readout in two colors. Finally, I will describe future research directions involving Nanopore-Plasmonics for rapid, single-molecule, proteins identification.