Our high quality and experienced bioanalytical services using the powerful technique of Surface Plasmon Resonance (SPR, Biacore) provides label-free, real time analysis of a pair of interacting molecules such as small molecule drugs binding to their target proteins. In more than 15 years Biobest acquired expert knowledge in application of Biacore SPR technology and has proven to be a reliable contractor for clients from pharmaceutical, research institutions and bio-diagnostic industry in supporting their specific projects. We especially have the experiences with a number of different SPR systems, such as Biacore 2000, Biacore 3000, Biacore X100. We can ensure a rapid and professional to assist to your samples analysis with tailor designed protocols as your specific requirements.

Learn Biacore from Publications

The mAbs 127 and 150 specifically bind to SARS-CoV-2 S1-RBD. (A) Affinity of mAbs 127 and 150 for S1-RBD. The S1-RBD-His-bound sensors were incubated with the different concentrations of mAbs 127 or 150 (indicated by different colors) for a set time interval to allow association. The sensors were then moved to protein-free solution and allowed to dissociate over a time interval. The binding kinetics were determined using Biacore T200 Evaluation Software version 3 with 1:1 binding model fitting. (Publication title as below and link)

Learn Biacore from Publications

Measuring the equilibrium dissociation constant (KD) of biomolecules with very fast binding on-rates and off-rates using a Biacore system often involves performing experiments at a series of suitable concentrations of the ligand. The crucial point is to allow the binding to reach equilibrium levels before starting the dissociation and then plot the equilibrium binding responses to determine the KD. See an example in the publication shown binding wasn’t reach equilibrium level in some of concentrations.

Fig.1 Assay set-up for the 14-3-3γ/SLP76 PPI. a) SPR binding assay of the SLP76-SH2 construct binding to 14-3-3γ in the presence of 5% DMSO. The KD value has been extrapolated from the binding curve reported on the right of the sensorgrams. (Publication title as below and link)

Learn Biacore from Publications

Baseline drifting in Biacore analysis refers to the slow, gradual shift in the baseline SPR signal that occurs over time during a biomolecular interaction analysis experiment. It is a common issue that can affect the accuracy and precision of the data obtained from a Biacore instrument. See an example in the following publication.

Fig.1g, IFNγ (left) or IFNγΔKRKR (right) was injected over an HS-activated surface (top) or an IFNγR1-activated surface (bottom) over 180 s, and the binding response in resonance units (RU) was recorded as a function of time. Each set of sensorgrams was obtained with IFNγ at (from bottom to top) 0, 25, 50, 75, 100, 150, 200 and 500 nM for the HS surface and at 0, 1, 2.5, 5, 10, 25 and 50 nM for the IFNγR1 surface. (Publication title as below and link)