Anti-VEGF drug interference with VEGF quantitation in the R&D systems human quantikine VEGF ELISA kit
| Autor: | Thomas DiCioccio, Nicholas J. Papadopoulos, Albert Torri, Thomas J. Daly, Giane Sumner, Camille Georgaros, Joel H. Martin, Ashique Rafique |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Vascular Endothelial Growth Factor A
genetic structures Bevacizumab medicine.drug_class VEGF receptors Clinical Biochemistry Angiogenesis Inhibitors Enzyme-Linked Immunosorbent Assay Monoclonal antibody 030226 pharmacology & pharmacy 01 natural sciences Analytical Chemistry 03 medical and health sciences 0302 clinical medicine medicine Drug interference Humans General Pharmacology Toxicology and Pharmaceutics Aflibercept Anti vegf biology medicine.diagnostic_test business.industry 010401 analytical chemistry General Medicine 0104 chemical sciences Medical Laboratory Technology Immunoassay biology.protein Cancer research Ranibizumab business medicine.drug |
| Zdroj: | Bioanalysis. 11:381-392 |
| ISSN: | 1757-6199 1757-6180 |
| Popis: | Aim: To evaluate the accuracy of the Quantikine Human VEGF Immunoassay (R&D Systems) in the presence of VEGF inhibitors. Materials & Methods: Quantikine VEGF ELISA (R&D), anti-VEGF165 mAb (R&D), VEGF165 and aflibercept (Regeneron), ranibizumab and bevacizumab (Genentech). Results: Binding affinity of anti-VEGF165 mAb for VEGF was threefold weaker than aflibercept, but 33- and 40-fold stronger than ranibizumab or bevacizumab. Extended incubation of VEGF complexed with inhibitors led to VEGF dissociation from ranibizumab and bevacizumab, but not aflibercept, and subsequent binding by the immunoassay capture antibody. The immunoassay also detected VEGF:ranibizumab and VEGF:bevacizumab complexes but not VEGF:aflibercept complexes. Conclusion: The immunoassay cannot accurately quantitate VEGF in the presence of these VEGF inhibitors as they interfere with the capture and detection of free VEGF. |
| Databáze: | OpenAIRE |
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