Abstract
Objective Rheumatoid arthritis (RA) is a systemic disease with chronic inflammation of the joints, and is caused by increased inflammatory cytokines such as TNF-α. The inhibition of TNF-α was found to effectively control inflammation, and block the progress of the disease. This study designed a new and efficient strategy to develop TNF-α antibodies. Methods Prokaryotic engineered cells were growing in a small scale bioreactor, and Fab' products (TMP5) were purified by affinity chromatography. Then TMP5 was modified by 20 kDa site-specific pegylation, and purified by SP sepharose column. Activities and affinities of TMP5 and PEG-TMP5 in vitro were studied. Results TMP5 was effectively produced after fermentation, periplasmic extraction and purification. The purity of TMP5 was more than 96%. After pegylation by 20 kDa PEG, the affinity and activity of PEG-TMP5 were (6.48±0.86)×10-9 M and (7.58±0.61)×10-11 M respectively, and were in the same range as positive controls. Conclusion PEG-TMP5 is a promising drug candidate for treating rheumatoid arthritis. Key words: Antibodies; Tumor necrosis factor α; Pegylation; pharmacology in vitro
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