Removal of autoantibodies by 4-mercaptoethylpyridine-based adsorbent

Amelioration of experimental autoimmune myasthenia gravis rats by blood purification treatment using 4‐mercaptoethylpyridine‐based adsorbent

“…MEP‐based adsorbents have been intensively studied for their ability to separate antibodies from complex feedstocks and are considered to be the most promising synthetic adsorbent that could substitute for protein A‐based adsorbents in the application of antibody purification 10–13. Our previous study explored the potential of MEP‐based adsorbent for immunadsorption application, and the synthesis procedure of the adsorbent was optimized based on its IgG adsorption capacity and selectivity obtained with human plasma 9. Sepharose CL‐6B was adopted as the solid matrix, because agarose bead is a physically and chemically stable resin, and has been used as a solid phase support matrix for several commercial immunoadsorbents used in plasmapheresis therapy.…”

“…1). 9 Briefly, Sepharose CL‐6B beads (10 g) were mixed with 2‐mL allyl bromide in 3 M sodium hydroxide solution (10 mL), and the mixture was shaken for 12 h at 30°C. Allyl‐activated Sepharose was then brominated with 1‐g N‐bromosuccinimide in 50% (w/v) acetone for 1 h at 30°C.…”

“…Important features of MEP‐based HCIC stationary phase are the near physiological working condition and its ability to capture antibodies directly from complex feedstock. In vitro studies employing human plasma samples have demonstrated the selectivity and reusability of MEP adsorbent for antibody adsorption, with the performances comparable to protein A adsorbent 9. In terms of its ability to remove pathogenic autoantibodies from the serum of different patients, MEP has shown a lower degree of variation in the treatment among the patients compared with protein A9 and is therefore a more superior adsorbent.…”

“…In vitro studies employing human plasma samples have demonstrated the selectivity and reusability of MEP adsorbent for antibody adsorption, with the performances comparable to protein A adsorbent 9. In terms of its ability to remove pathogenic autoantibodies from the serum of different patients, MEP has shown a lower degree of variation in the treatment among the patients compared with protein A9 and is therefore a more superior adsorbent. In this study, in vivo investigation with experimental autoimmune MG (EAMG) rat model was conducted to further assess the safety and efficacy of MEP adsorbent for the treatment of MG.…”

Influences of Ligand Structure and pH on the Adsorption with Hydrophobic Charge Induction Adsorbents: A Case Study of Antibody IgY

“…The protein can be adsorbed at neutral pH by the thiophilic and hydrophobic interactions with sulfur atom and pyridine ring on the ligand, and desorbed under the electrostatic repulsion between the protein and the charged ligands when the pH is less than the pK a of MEP and pI of the target protein (16). It was found that HCIC ligands could bind selectively to the Fc domains of immunoglobulin and showed a potential application for antibody purification as the cost-effective alternative to Protein A affinity chromatography (17)(18)(19)(20)(21). Due to the multimodal interactions between the HCIC ligand and the target protein, the adsorption and separation behaviors are quite complicated and the design of the ligand is often empirical.…”