Immunological agglutination kinetics of latex particles with covalently immobilized antigens |
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| Affiliation: | 1. Department of Chemistry, University of Virginia, Charlottesville, VA, 22904, USA;2. TeGrex Technologies, Charlottesville, VA, 22904, USA;3. Department of Mechanical and Aerospace Engineering, University of Virginia, Charlottesville, VA, 22904, USA;4. Department of Pathology, University of Virginia, Charlottesville, VA, 22904, USA;1. Nanobiosensors and Bioanalytical Applications Group (NanoB2A), Catalan Institute of Nanoscience and Nanotechnology (ICN2), CSIC and the Barcelona Institute of Science and Technology, 08193 Bellaterra, Barcelona, Spain;2. CIBER-BBN Networking Center on Bioengineering, Biomaterials and Nanomedicine, Spain;3. Protein Alternatives, S.L., Tres Cantos, Madrid, Spain;1. School of Science and Engineering, Teesside University, Borough Road, Middlesbrough TS1 3BA, United Kingdom;2. Graduate Research School, Teesside University, Borough Road, Middlesbrough TS1 3BA, United Kingdom;1. Institute of Antibody Engineering, School of Laboratory Medicine and Biotechnology, Southern Medical University, 1023 South Shatai Road, Guangzhou, 510515, China;2. National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China;3. Department of Liver Disease, Guangdong Hospital of Traditional Chinese Medicine (Zhuhai), 53 Jingle Road, Zhuhai, 519015, China;4. Center of Electron Microscopy, Central Laboratory, Southern Medical University, 1023 South Shatai Road, Guangzhou, 510515, China;5. State Key Laboratory of Biocontrol, School of Life sciences, Sun Yat-sen university, 135 Xingang Xi Road, Guangzhou, 510275, China;6. College of Life Sciences, University of Chinese Academy of Sciences, Beijing, 100049, China;7. Department of TCM, Shenzhen Hospital of Southern Medical University, 1333 Xinhu Road, Shenzhen, 518101, China |
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| Abstract: | Hen egg-white lysozyme (HEL), ovalbumin and bovine serum albumin (BSA) were covalently immobilized onto styrene/methacrylic acid [P(St/MAA)] copolymer latex particles by the carbodiimide method. The initial rates of the immunological agglutination of these particles initiated by the addition of antibodies were quantified by the absorbance changes at a wavelength of 680 nm. The sensitivity of the immunological agglutination of the particles with covalently immobilized antigens was higher than that with physically adsorbed ones. The immunological agglutination kinetics showed a similar tendency irrespective of antigen-antibody systems. That is, the initial agglutination rates (i) increased with increasing immobilized amount of antigens, (ii) were largest in the ionic strength range of 0.02 to 0.05 at pH 7 and (iii) decreased with increasing pH. These results indicate that the electrostatic interactions of particle-particle and particle-antibody are main factors which control the immunological agglutination. On the other hand, the sensitivity of the immunological agglutination increased with increasing molecular size of antigens. |
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