02022nas a2200253   4500008004100000022001400041245010800055210006900163260000900232300001100241490000700252520118300259653002301442653002901465653001501494653002601509653001401535100002001549700001701569700001901586700002001605700002001625856012301645       2020                        eng d  a0734-975000aEngineering staphylococcal protein A for high-throughput affinity purification of monoclonal antibodies0 aEngineering staphylococcal protein A for highthroughput affinity  cNOV   a1076320 v443 a<p>Protein A chromatography is one of the most widely used purification steps in the manufacturing of the various classes of recombinant and non-recombinant antibodies. Due to the higher cost, lower binding capacity, and limited life cycle of Protein A ligand, this affinity-based purification step is often one of the most significant contributors to the cost of manufacturing of monoclonal antibody (mAb) products. In the last decade, there has been significant progress in improving the Protein A chromatography throughput by designing new engineered Staphylococcal Protein A (SPA) variants with higher dynamic binding capacity, considerable alkaline tolerance, and mild acidic elution pH. This review aims at summarizing the various protein engineering approaches used for improving the throughput of the Protein A-based affinity purification of various immunoglobulins. With biopharmaceutical producers operating under ever-increasing pressure towards reducing the cost of manufacturing, these advances in engineered protein A variants will help in processing larger cell culture volumes with high throughput and thereby significantly lower the cost of raw materials.</p>
10aAlkaline tolerance10aDynamic binding capacity10aElution pH10aMonoclonal antibodies10aProtein A1 aAmritkar, Vinod1 aAdat, Satish1 aTejwani, Vijay1 aRathore, Anurag1 aBhambure, Rahul  uhttps://library.ncl.res.in/content/engineering-staphylococcal-protein-high-throughput-affinity-purification-monoclonal02210nas a2200265   4500008004100000022001400041245011100055210006900166260000800235300001400243490000700257520132700264653001501591653003001606653002601636653001401662653001501676100002601691700002001717700002501737700001801762700001901780700001701799856012801816       2022                        eng d  a0268-257500aMechanistic modeling of continuous capture step purification of biosimilar monoclonal antibody therapeutic0 aMechanistic modeling of continuous capture step purification of   cSEP  a2404-24190 v973 a<p>
	{BACKGROUND Continuous multicolumn Protein A chromatography offers various advantages for capture stage purification of monoclonal antibody therapeutics, like higher productivity and resin capacity utilization, lower buffer consumption, small footprint, etc. Due to the complexity of the continuous process, experimental optimization is time-consuming and cost-intensive. This investigation proposes a hybrid process development approach integrating experimental and mechanistic modeling for time- and cost-effective development and optimization of continuous Protein A affinity chromatography. RESULTS Productivity and capacity utilization of the continuous CaptureSMB process under varying operating conditions were predicted using the Chromatography Analysis and Design Toolkit (CADET) framework and validated with experimental results. Effects of critical process parameters like feed concentration (c(0)), loading breakthrough (s) and residence time (RT) on productivity and capacity utilization were evaluated. Model predictions were validated using the experimental results proving the reliability and feasibility of the modeling approach. At 15.00 +/- 0.20 mg mL(-1) feed model mAb concentration, the model-based approach predicted the best performance giving 27.56 g L-1 h(-1) productivity (RT = 2 min</p>
10aCaptureSMB10acontinuous chromatography10aMathematical modeling10aProtein A10asimulation1 aDeulgaonkar, Prashant1 aBhambure, Rahul1 aPrasad, Bhaskarjyoti1 aMishra, Ashok1 aTiwari, Sanjay1 aMody, Rustom  uhttps://library.ncl.res.in/content/mechanistic-modeling-continuous-capture-step-purification-biosimilar-monoclonal-antibody