Sensorgram

Fig.Sa-f. The sensorgram of the repeated injection of the aqueous viologen dimer 2 (a, c, e) and the antibody (b, d, f) solutions. [Viologen dimer 2]=2.0 pM and [antibody]=2.0 pM in phosphate borate buffer. Injection period 60 s for a-c and 120 s for d-f. A solution of viologen dimer 2 or the antibody passes over the surface of the sensor chip for 60 or 120 s at a constant flow rate of 20 pL min. The surface of the sensor chip was subsequently washed with buffer...

Fig. 12a,b. The sensorgrams for the binding of the antibody dendrimer (a) or IgG (b) to the anionic porphyrin immobilized onto the surface of the sensor chip. Phosphate borate buffer (0.1 M, pH 9.0) was used. TCPP was immobilized via hexamethylenediamine spacer onto the sensor chip and then a solution of IgG or the dendrimer was injected to the flow cell. After 60 s from the injection of the antibody solutions, flow ceU was filled with buffer... 

By continuously monitoring the SPR response, e q)ressed in resonance units (RU), in the detected volume and plotting this value against time a sensorgram is obtained. 

The sensorgram can be divided into three phases association during sancple injection, steady-state where the rate of analyte binding is balanced by dissociation from the complex and dissociation from the surface diming buffer flow at the end of sarrqile injection (Fig. 1). 

Sensorgrams for the interaction of PGEP with different amounts of F. moniliforme PG are own in fig. 2. The increase in RU from the initial baseline represents the binding of the PG to the surfrice-bound PGIP. The plateau line represoits the steady state phase of the PG-PGIP interaction Me the decrease in RU at the td of the injection represents the dissociation phase. 

Fig. 2. Sensorgrams of Fusarium moniliforme enddPG injected over a PGIP surface at different concentrations.

Kinetics evaluation software generates the values of ka (rates of complex formation) and kd (rates of complex dissociation) by fitting the data to interaction models. In a sensorgram, if binding occurs as sample passes over a prepared sensor surface, the response increases and is registered upon equilibrium, a constant signal is reached. The signal decreases when the sample is replaced with buffer, since the bound molecules dissociate. 

Fig. 6.9 OERR response to various part per million (ppm) concentrations of ethanol and hexane vapors. The OERR is coated with a 200 nm thick OV 17 (a) and PEG 400 (b). Insets are the sensorgrams taken by monitoring the WGM shift in real time. Reprinted from Ref. 28 with permission. 2008 Optical Society of America...

In Fig. 15.7, four sensorgrams are shown for air and water cover media and for TE/TM polarized light. The peaks are correctly centred at the angles given by the grating equation sin(oco) No A/A and the half-widths are approximately 0.05°. It is seen that the shift in peak position from air to water is largest for the TM mode, which is due to the fact that the TM mode is closest to cutoff and therefore exhibit the largest sensitivity. 

Fig. 15.20 RI sensorgram for 1, 3 and 7 x 105 spores per mL of bacteria using PT CLW sensor. Arrows indicate the times at which various solutions were added. Reprinted from Ref. 24 with permission. 2008 Elsevier...

Fig. 15.21 Peak type detection of HaCaT cells settling onto the sensor surface, (a) Three sensorgrams obtained after 40, 90 and 200 min (b) angular position of the peak vs. time and (c) microscope image of the exposed sensor surface taken right after the measurements. The area shown is 460 x 400 pm2. Reprinted from Ref. 27 with permission. 2008 Elsevier...

Fig. 3 SPR sensorgrams. Upper Binding curves of 20 pg/mL of BclA to immobilized PAA-mannose in the presence of (A) 1.95 pM-0.25 mM a-benzyl-mannoside (the best ligand from tested monosaccharides) and (B) 0.95 mM-25 mM D-galactose (non-binder). Bottom SPR sensorgrams for D-mannose binding to immobilized BclA. (C) Equilibrium steady state curves for D-mannose varying from 1 to 500 pM. (D) The corresponding binding curve derived from steady-state equilibrium values.

Fig. 4. Sensorgram of injection of biotinylated Florse Radish Peroxidase (b-FIRP) (10 pg/ml).

Fig. 6 a General waveguide sensor configuration b typical sensorgram... 

Fig. 14 TE and TM sensorgrams for the nanoporous waveguide using air and water as cover media [28]...

Fig. 18 a TE and TM sensorgrams obtained before and after cell attachment to the waveguide surface, b Mean TE and TM peak positions versus time after exposing the waveguide surface to the cell solution... 

Fig. 20 TE and TM sensorgrams for the nanoporous waveguide obtained for the cover RIs a 1.331, b 1.342, c 1.354, d 1.363, e 1.373,/ 1.383, andg 1.403. The cover consists of water with various concentrations of NaSCN [34]...

Fig. 22 Thin-plate waveguide sensorgrams obtained with a grating-coupled, 52- im-thick glass plate for three different aqueous cover media, tic = 1-331 (pure water), 1.342 (water with 5% NaSCN), and 1.354 (water with 10% NaSCN) [35]...

Fig. 2 Schematic of real-time biointerface upon analyte binding to sensing surface. The reflectivity curve lower left) shifts upon analyte binding (displayed as AB) and can be monitored in realtime with a sensorgram lower right)...

The SPR sensorgram generally contains three phases the association phase, the dissociation phase, and the regeneration phase, as shown in detail in Fig. 3. The binding kinetics that quantitatively characterizes a bio-molecular interaction by rate constants and equilibrium constants can be determined from the sensorgram. 

Fig. 3 Sample SPR sensorgram showing all the different kinetics phases along with key fimctional...

Fig. 5 Characteristic sensorgram for carbohydrate functionalized sensing surface in response to 400 pg/ mLSNA...

To evaluate whether this unusual behaviour was characteristic of this particular recombinant IL-bp), another recombinant IL-6 preparation, termed IL-6m was utilised. Sensorgrams describing IL-6j binding to immobilised... 

Fig. 2 Sensorgrams of CM5/anti-human myoglobin IgG/HSA myoglobin system. (A) Covalent immobilization of IgG to flow cells. A sensorgram reading of 15,000 RU is indicated corresponding to an antibody binding capacity of - 200 finol myoglobin. (B) Myoglobin retained by flow cells 2 (FC2), and 3 (FC3). Retention of 20 fmol, and 10 fmol, of myoglobin is indicated for flow cells 2, and 3, respectively.

For competition studies, the Fab fragment was chemically coupled to the BIAcore chip and wild type rhIL-ip was used as analyte. Figure 1 presents the BIAcore sensorgrams obtained when different concentrations of wild type rhIL-ip (0.6-29 nM) were passed sequentially over the immobilized Fab chip. 

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