Limitation of tuning the antibody-antigen reaction by changing the value of pH and its consequence for hyperthermia
| Autor: | J. Mleczko, T.T. Nguyen, Alicja Defort, Julia Nowak-Jary, Bartlomiej Zapotoczny, Maciej Marć, Agnieszka Mironczyk, Ewelina Gronczewska, Jacek J. Kozioł, Mirosław R. Dudek |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
Immunoglobulin A Hot Temperature Antibody Affinity Enzyme-Linked Immunosorbent Assay Biochemistry Antibodies Antigen-Antibody Reactions Immunoglobulin Fab Fragments 03 medical and health sciences Antigen medicine Humans Isoelectric Point Antigens Magnetite Nanoparticles Saliva Molecular Biology Chromatography medicine.diagnostic_test biology Chemistry Regular Papers General Medicine Hydrogen-Ion Concentration 030104 developmental biology Isoelectric point Magnetic hyperthermia Immunoassay biology.protein Magnetic nanoparticles Antibody |
| Zdroj: | Journal of Biochemistry. 159:421-427 |
| ISSN: | 1756-2651 0021-924X |
| DOI: | 10.1093/jb/mvv120 |
| Popis: | Distribution of the isoelectric point (pI) was calculated for the hypervariable regions of Fab fragments of the antibody molecules, which structure is annotated in the structural antibody database SabDab. The distribution is consistent with the universal for all organisms dividing the proteome into two sets of acidic and basic proteins. It shows the additional fine structure in a form of the narrow-sized peaks of pI values. This is an explanation why a small change of the environmental pH can have a strong effect on the antibody-antigen affinity. To show this, a typical enzyme-linked immunospecific assay experiment for testing the reaction of goat anti-human IgA antibodies with human IgA immunoglobulins of saliva as antigens was modified in such a way that Fe3O4 magnetic nanoparticles were added to PBS buffer. The magnetic nanoparticles were remotely heated by the radio frequency magnetic field providing the local change of temperature and pH. It was observed that short times of the heating were significantly increasing the antibody-antigen binding strength while it was not the case for a longer time. The finding discussed in the study can be useful for biopharmaceuticals using antibodies, the immunoassay techniques as well as for control over the use of hyperthermia. |
| Databáze: | OpenAIRE |
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