The Experts below are selected from a list of 412167 Experts worldwide ranked by ideXlab platform
Yuanyuan Zhao - One of the best experts on this subject based on the ideXlab platform.
-
biomolecular interaction analysis using an Optical Surface plasmon resonance biosensor the marquardt algorithm vs newton iteration algorithm
PLOS ONE, 2015Co-Authors: Jiandong Hu, Xinran Hu, Ruipeng Chen, Shun Wang, Keke Chang, Min Jiang, Jianming Yang, Yuanyuan ZhaoAbstract:Kinetic analysis of biomolecular interactions are powerfully used to quantify the binding kinetic constants for the determination of a complex formed or dissociated within a given time span. Surface plasmon resonance biosensors provide an essential approach in the analysis of the biomolecular interactions including the interaction process of antigen-antibody and receptors-ligand. The binding affinity of the antibody to the antigen (or the receptor to the ligand) reflects the biological activities of the control antibodies (or receptors) and the corresponding immune signal responses in the pathologic process. Moreover, both the association rate and dissociation rate of the receptor to ligand are the substantial parameters for the study of signal transmission between cells. A number of experimental data may lead to complicated real-time curves that do not fit well to the kinetic model. This paper presented an analysis approach of biomolecular interactions established by utilizing the Marquardt algorithm. This algorithm was intensively considered to implement in the homemade bioanalyzer to perform the nonlinear curve-fitting of the association and disassociation process of the receptor to ligand. Compared with the results from the Newton iteration algorithm, it shows that the Marquardt algorithm does not only reduce the dependence of the initial value to avoid the divergence but also can greatly reduce the iterative regression times. The association and dissociation rate constants, ka, kd and the affinity parameters for the biomolecular interaction, KA, KD, were experimentally obtained 6.969×105 mL·g-1·s-1, 0.00073 s-1, 9.5466×108 mL·g-1 and 1.0475×10-9 g·mL-1, respectively from the injection of the HBsAg solution with the concentration of 16ng·mL-1. The kinetic constants were evaluated distinctly by using the obtained data from the curve-fitting results.
-
evaluation of kinetic constants of biomolecular interaction on Optical Surface plasmon resonance sensor with newton iteration method
5th International Symposium on Advanced Optical Manufacturing and Testing Technologies: Optical Test and Measurement Technology and Equipment, 2010Co-Authors: Yuanyuan Zhao, Guoliang Jiang, Jianguang Wei, Liang ShiAbstract:ABSTRACT In the immunology, there are two important types of biomolecular interaction: an tigens-antibodies and receptors-ligands. Monitoring the response rate and affinity of biomolecular interaction can help analyze the protein function, drug discover, genomics and proteomics research. Moreover the association rate constant and dissociation rate constant of receptors-ligands are the important parameters for the study of signal transmission between cells. Recent advances in bioanalyzer instruments have greatly simplified the measurement of the kinetics of molecular interactions. Non-destructive and real-time monitoring the response to evaluate the parameters between antigens and antibodies can be performed by using Optical Surface plasmon resonance (SPR) biosensor technology. This technology provides a quantitative analysis that is carried out rapidly with label-free high-throughput detection using the binding curves of antigens-antibodies. Consequently, the kinetic parameters of interaction between antigens and antibodies can be obtained. This article presents a low cost integrated SPR-based bioanalyzer (HPSPR-6000) designed by ourselves. This bioanalyzer is mainly composed of a biosensor TSPR1K23, a touch-screen monitor, a microprocessor PIC24F128, a microflow cell with three channels, a clamp and a photoelectric conversion device. To obtain the kinetic parameters, sensorgrams may be modeled using one of several binding mode ls provided with BIAevaluation software 3.0, SensiQ or Autolab. This allows calculation of the association rate consta nt (ka) and the dissociation rate constant (kd). The ratio of ka to kd can be used to estimate the equilibrium constant. Another kind is the analysis software OriginPro, which can process the obtained data by nonlinear fitting and then get some correlative parameters, but it cant be embedded into the bioanalyzer, so the bioanalyzer dont support the use of OriginPro. This paper proposes a novel method to evaluate the kinetic parameters of biomolecular interaction by using Newton Iteration Method and Least Squares Method. First, the pseudo first order kinetic model of biomolecular interaction was established. Then the data of molecular interaction of HBsAg and HBsAb was obtained by bioanalyzer. Finally, we used the Optical SPR bioanalyzer software which was written by ourselves to make nonlinear fit about the association and dissociation curves. The correlation coefficient R-squared is 0.99229 and 0.99593, respectively. Furthermore, the kinetic parameters and affinity constants were evaluated using the obtained data from the fitting results. Keyword: Biomolecular interaction, kinetic model, cu rve fitting arithmetic, Surface plasmon resonance
Ramadan A. Abuknesha - One of the best experts on this subject based on the ideXlab platform.
-
Integrated Optical Surface plasmon resonance immunoprobe for simazine detection
Biosensors and Bioelectronics, 1999Co-Authors: R. D. Harris, B.j Luff, Arne Brecht, GERHARD GAUGLITZ, J S Wilkinson, Jacob Piehler, Ramadan A. AbukneshaAbstract:This paper presents the detailed design and characterisation of a regenerable integrated Optical Surface plasmon resonance immunoprobe as a detector for the triazine herbicide simazine. A sensor design theoretically optimised for use in the aqueous environment is presented and its fabrication described. Experimental results on the sensitivity to changes in bulk refractive index of the analyte and on non-specific binding of ovalbumin are presented. Binding inhibition immunoassays were conducted for simazine and the lower limit of detection determined to be 0.16 μg/l using anti-simazine IgG antibodies and 0.11 μg/l using anti-simazine Fab fragments. A sample test cycle of 20 min was established.
Aldert A Bergwerff - One of the best experts on this subject based on the ideXlab platform.
-
immunochemical detection of salmonella group b d and e using an Optical Surface plasmon resonance biosensor
Fems Microbiology Letters, 2003Co-Authors: G C A M Bokken, Ronald J Corbee, Frans Van Knapen, Aldert A BergwerffAbstract:A Surface plasmon resonance biosensor (Biacore) was used to detect Salmonella through antibodies reacting with Salmonella group A, B, D and E (Kauffmann–White typing). In the assay designed, anti-Salmonella antibodies immobilized to the biosensor Surface were allowed to bind injected bacteria followed by a pulse with soluble anti-Salmonella immunoglobulins to intensify the signal. No significant interference was found for (mixtures of) 30 non-Salmonella serovars at 109 CFU ml−1. A total of 53 Salmonella serovars were successfully detected at 1×107 CFU ml−1, except those of groups C, G, L and P, as expected. The cut-off point was determined with an equicellular mixture of Salmonella enteritidis and Salmonella typhimurium at a final amount of 1.7×103 CFU per test portion. Although further work is needed to cover the detection of all relevant Salmonella serovars in food-producing animals and food products, this work demonstrates the merits of this alternative biosensor approach in terms of automation, sensitivity, specificity, simple handling and limited hands-on time.
E V Alieva - One of the best experts on this subject based on the ideXlab platform.
-
photonic crystal biosensor based on Optical Surface waves
Sensors, 2013Co-Authors: Valery N Konopsky, E V Alieva, Tanya Karakouz, Chiara Vicario, S K Sekatskii, Giovanni DietlerAbstract:A label-free biosensor device based on registration of photonic crystal Surface waves is described. Angular interrogation of the Optical Surface wave resonance is used to detect changes in the thickness of an adsorbed layer, while an additional simultaneous detection of the critical angle of total internal reflection provides independent data of the liquid refractive index. The abilities of the device are demonstrated by measuring of biotin molecule binding to a streptavidin monolayer, and by measuring association and dissociation kinetics of immunoglobulin G proteins. Additionally, deposition of PSS / PAH polyelectrolytes is recorded in situ resulting calculation of PSS and PAH monolayer thicknesses separately.
-
photonic crystal Surface waves for Optical biosensors
Analytical Chemistry, 2007Co-Authors: Valery N Konopsky, E V AlievaAbstract:We present a new Optical biosensor technique based on registration of dual Optical s-polarized modes on a photonic crystal Surface. The simultaneous registration of two Optical Surface waves with different evanescent depths from the same Surface spot permits the segregation of the volume and the Surface contributions from an analyte, while the absence of metal damping permits an increase in the propagation length of the Optical Surface waves and the sensitivity of the biosensor. Our technique was tested with the binding of biotin molecules to a streptavidin monolayer that has been detected with signal/noise ratio of approximately 15 at 1-s signal accumulation time. The detection limit is approximately 20 fg of the analyte on the probed spot of the Surface.
Valery N Konopsky - One of the best experts on this subject based on the ideXlab platform.
-
photonic crystal biosensor based on Optical Surface waves
Sensors, 2013Co-Authors: Valery N Konopsky, E V Alieva, Tanya Karakouz, Chiara Vicario, S K Sekatskii, Giovanni DietlerAbstract:A label-free biosensor device based on registration of photonic crystal Surface waves is described. Angular interrogation of the Optical Surface wave resonance is used to detect changes in the thickness of an adsorbed layer, while an additional simultaneous detection of the critical angle of total internal reflection provides independent data of the liquid refractive index. The abilities of the device are demonstrated by measuring of biotin molecule binding to a streptavidin monolayer, and by measuring association and dissociation kinetics of immunoglobulin G proteins. Additionally, deposition of PSS / PAH polyelectrolytes is recorded in situ resulting calculation of PSS and PAH monolayer thicknesses separately.
-
photonic crystal Surface waves for Optical biosensors
Analytical Chemistry, 2007Co-Authors: Valery N Konopsky, E V AlievaAbstract:We present a new Optical biosensor technique based on registration of dual Optical s-polarized modes on a photonic crystal Surface. The simultaneous registration of two Optical Surface waves with different evanescent depths from the same Surface spot permits the segregation of the volume and the Surface contributions from an analyte, while the absence of metal damping permits an increase in the propagation length of the Optical Surface waves and the sensitivity of the biosensor. Our technique was tested with the binding of biotin molecules to a streptavidin monolayer that has been detected with signal/noise ratio of approximately 15 at 1-s signal accumulation time. The detection limit is approximately 20 fg of the analyte on the probed spot of the Surface.