scholarly journals Investigation of Antigen-Antibody Interactions of Sulfonamides with a Monoclonal Antibody in a Fluorescence Polarization Immunoassay Using 3D-QSAR Models

2012 ◽  
Vol 13 (5) ◽  
pp. 6334-6351 ◽  
Author(s):  
Zhanhui Wang ◽  
Zhenpeng Kai ◽  
Ross C. Beier ◽  
Jianzhong Shen ◽  
Xinling Yang
Keyword(s):  
Monoclonal Antibody ◽  
Fluorescence Polarization ◽  
3D Qsar ◽  
Fluorescence Polarization Immunoassay ◽  
Qsar Models ◽  
Antigen Antibody ◽  
Antibody Interactions

Monoclonal Fluorescence Polarization Immunoassay Evaluated for Monitoring Cyclosporine in Whole Blood After Kidney, Heart, and Liver Transplantation

1992 ◽  
Vol 38 (1) ◽  
pp. 123-126 ◽  
Author(s):  
M Winkler ◽  
G Schumann ◽  
D Petersen ◽  
M Oellerich ◽  
K Wonigeit
Keyword(s):  
Monoclonal Antibody ◽  
Liver Transplantation ◽  
Whole Blood ◽  
Fluorescence Polarization ◽  
Fluorescence Polarization Immunoassay ◽  
Transplant Patients ◽  
Specific Radioimmunoassay ◽  
Metabolite Concentrations ◽  
A Prospective Study

Abstract In a prospective study we evaluated a novel fluorescence polarization immunoassay (FPIA) for determining cyclosporine (CsA) in whole blood. FPIA uses a monoclonal antibody and is performed on the TDx (Abbott). The within-series (CV less than 2%) and between-days (CV less than 3.3%) precision of the assay was excellent. The results obtained by the monoclonal FPIA in samples from transplant patients (n = 100) averaged 31.9% and 20.2% higher than those by HPLC and a specific radioimmunoassay (INCStar), respectively. Results by all three methods correlated well. Follow-up studies during the early course after liver transplantation, however, suggested that high metabolite concentrations affect FPIA results. This is explained by previously described cross-reactions of the monoclonal antibody with some CsA metabolites. The FPIA results in samples of such patients should be interpreted cautiously.

Fluorescence polarization immunoassay based on a new monoclonal antibody for the detection of the Diisobutyl phthalate in Yoghurt

Food Control ◽  
2019 ◽  
Vol 105 ◽  
pp. 38-44 ◽  
Author(s):  
Yingshan Chen ◽  
Qiyi He ◽  
Ding Shen ◽  
Zhengyun Jiang ◽  
Sergei A. Eremin ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Fluorescence Polarization ◽  
Fluorescence Polarization Immunoassay

scholarly journals Molecular Docking and Molecular Dynamics (MD) Simulation of Human Anti Complement Factor H (CFH) Antibody Ab42 and CFH Polypeptide (pCFH)

2018 ◽  
Author(s):  
Bing Yang ◽  
Jiayi Ren ◽  
Tong Liu ◽  
Shujian Lin ◽  
Yueming Wang ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Molecular Docking ◽  
Md Simulation ◽  
Factor H ◽  
Energy Calculation ◽  
Complement Factor ◽  
Alanine Scanning ◽  
Computational Alanine Scanning ◽  
Antigen Antibody ◽  
Antibody Interactions

The details of antigen-antibody interactions and the identification of epitopes are critical for the development of monoclonal antibody drugs. Ab42 is a native human-derived anti-CFH monoclonal antibody. In this study, the interaction between antigen pCFH and antibody (Ab42) was theoretically demonstrated by molecular docking and MD simulation, combined with free energy calculation and computational alanine scanning (CAS), and key amino acids and epitopes were identified. Experimental alanine scanning (EAS) was then carried out to verify the results of the calculation, and our results indicated that Ab42 antibody forms hydrogen bonds and interacts hydrophobically with pCFH through the Tyr315, Ser100, Gly33, and Tyr53 residues on its CDR, while the main pCFH epitopes are located at the six sites of Pro441, Ile442, Asp443, Asn444, Ile447, and Thr448. In conclusion, this study has explored the mechanism of antigen-antibody interaction from both theoretical and experimental aspects, and our results have important theoretical significance for the design and development of relevant antibody drugs.

scholarly journals A fluorescence polarization immunoassay for the rapid detection of antibody against influenza A virus in chicken and goat sera

2020 ◽  
Vol 32 (6) ◽  
pp. 887-891
Author(s):  
Yohei Takeda ◽  
Yutaka Yonezawa ◽  
Satoshi Asake ◽  
Haruko Ogawa ◽  
Kunitoshi Imai
Keyword(s):  
Fluorescence Polarization ◽  
Influenza A ◽  
Rapid Test ◽  
Infectious Agent ◽  
Fluorescence Polarization Immunoassay ◽  
Influenza A Viruses ◽  
Highly Pathogenic ◽  
One Step ◽  
H5 Subtype ◽  
Antigen Antibody

Highly pathogenic influenza A viruses (IAVs) cause substantial damage to the poultry industry. A simple and quick testing method is required for strict control of this infectious agent. The fluorescence polarization immunoassay (FPIA) is a rapid test based on antigen–antibody binding, which can detect antigen-specific antibody in the infected animal samples within a few minutes. FPIA is a one-step reaction assay that does not require a secondary antibody and complicated steps. We evaluated the usefulness of FPIA for the detection of anti-IAV antibodies, including those against internal proteins and H5 subtype HA, in sera. In the FPIA using fluorescent peptides of internal NP and M1 proteins, millipolarization units (MPUs), which increase depending on the amount of antibody, were higher in antibody-positive sera than in antibody-negative sera. Moreover, in FPIA using fluorescent recombinant H5 subtype HA proteins, anti-H5 serum gave the highest MPUs among the antisera raised in goats against individual H1–H15 subtype IAVs. Our results support the utility of FPIA for the detection of anti-IAV antibodies, especially the anti-H5 antibody.

Monoclonal Antibody-Based Fluorescence Polarization Immunoassay for Sulfamethoxypyridazine and Sulfachloropyridazine

2007 ◽  
Vol 55 (17) ◽  
pp. 6871-6878 ◽  
Author(s):  
Zhanhui Wang ◽  
Suxia Zhang ◽  
Irina S. Nesterenko ◽  
Sergei A. Eremin ◽  
Jianzhong Shen
Keyword(s):  
Monoclonal Antibody ◽  
Fluorescence Polarization ◽  
Fluorescence Polarization Immunoassay
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