Optimer beacons of accuracy in small molecule analytics
Optimer beacons are reagents for simple, solution-based detection and analysis of target concentration.
These beacons work by binding to specific analytes in a solution, resulting in a fluorescent signal. This signal can then be detected and quantified, providing an accurate and concentration-dependent assay for the specific analyte. The versatility of Optimer beacons spans research, including in live cells to localise and quantify molecules in cell processes, in bioprocessing to monitor process performance by quantifying specific process ingredients, in food and environmental monitoring, as well as in diagnostics.
Using Optimer beacons with a convenient fluorescent readout gives you the vital benefits of:
- A simple, solution-based assay format that cuts extra incubations and wash steps.
- Ability for field-based detection and monitoring using a simple handheld reader.
- Potential for multiplexed assays using Optimer with a diverse array of fluorophores.
But why use Optimer for beacons?
Optimer beacons rely on the conformational change that occurs when Optimers bind to small molecule targets. As Optimers have a flexible backbone, they typically wrap around small molecule analytes, offering accuracy in detection. This flexible backbone makes beacon assay reagents possible with Optimer and sets them apart from alternative affinity reagents. Unlike the rigid structures found in protein-based affinity reagents such as antibodies, peptides, and MIPs, Optimer’s flexibility enables the creation of beacon assay reagents with ease.
How do Optimer beacons work?
For Optimer beacons, the Optimer binder is labelled with a fluorophore and a quencher (to give a gain of signal) or a FRET pair of fluorophores (to give a colour change). As the Optimer beacon binds the small molecule target the induced conformational change increases the distance between the two labels.
For the fluorophore and quencher pairing, the signal from the fluorophore remains suppressed when the Optimer beacon is not bound to the target. However, upon binding, the conformational change separates the fluorophore from the quencher, resulting in a detectable fluorescent signal.
Alternatively, with a FRET pair, the conformational change of the Optimer when binding the target increases the distance between the two fluorophores. This alteration inhibits non-radiative energy transfer, leading to a shift in fluorescence detectable by a change in colour.
Orthogonal assays with Optimer beacons
Our Optimer discovery process for small molecule targets is ideal for beacon development. The initial binder discovery is performed in solution, meaning that the Optimer binders are engineered to interact with and detect the analyte in solution, matching your assay format for better performance.
Optimer beacons can be developed directly as beacon reporters. However, if you have a small molecule binding Optimer, we have engineered processes that allow the same binder to be adapted to function as an Optimer beacon. The capability to change your Optimer binder into a beacon allows you to work with the Optimer as an affinity reagent for standard assays like ELONA and, in parallel, as a beacon. Being able to use your Optimer in these ways offers the potential for orthogonal assays for small molecule analysis.
While immunoassays like ELISAs can be useful for sensitive detection and quantification of targets in complex matrices, these assays can be time and labour intensive, with multiple incubation and wash steps. The introduction of Optimer beacons can remove the requirement for multiple wash steps in these assays, while keeping the sensitive and selective detection you need.
To learn about our Optimer discovery process for small molecule targets or to see how we have been able to adapt Optimer binders into Optimer beacons for small molecule targets, join our upcoming webinar.