High productivity purification of immunoglobulin G monoclonal antibodies on starch-coated magnetic nanoparticles by steric exclusion of polyethylene glycol

Gagnon, Pete; Toh, Phyllicia; Lee, Jeremy

doi:10.1016/j.chroma.2013.11.039

Cited by 42 publications

(42 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…More recently, Gagnon et al [119] reported 69% of IgG recovery with more than 99% removal of HCP using magnetic starch-coated nanoparticles. Taking into account all the information mentioned before, it can be concluded that magnetic separation consists in a fast and smooth process, which combines the capability of scale-up with the possibility of automation, allows the separation and purification of mAbs in few minutes, and once the contaminants are tolerated, there is no need to perform any filtration or centrifugation prior to sample loading, which supports the potential of this technique for mAbs purification.…”

Section: Nimentioning

confidence: 99%

Monoclonal Antibodies - Addressing the Challenges on the Manufacturing Processing of an Advanced Class of Therapeutic Agents

Capela¹,

Aires‐Barros²,

Freire³

et al. 2017

Frontiers in Clinical Drug Research: Anti-Infectives Volume 4

View full text Add to dashboard Cite

Monoclonal antibodies (mAbs) were firstly described by Köhler and Milstein in 1975, and their potential as powerful therapeutic agents recognized in the following years. Currently, the US Food and Drug Administration (FDA) has already approved 56 monoclonal antibodies for the treatment of several diseases, including cancer (e.g. breast cancer, leukemia and prostate cancer), auto-immune disorders (rheumatoid arthritis and Crohn's disease), asthma, and cardiovascular and infectious diseases. Despite their advantages and therapeutic potential, the cost of manufacturing these biopharmaceuticals with high quality and purity level is still extremely high due to the absence of current cost-effective extraction/purification methods, and which has also impaired their widespread application as recurrent therapeutic agents. The upstream processing of mAbs has gone through several improvements in recent years, by using alternative expression systems or by optimizing the medium formulations and feeding strategies. On the contrary, the downstream processing is considered the bottleneck in the manufacturing of mAbs for therapeutic purposes at reliable costs, representing up to 80% of their total production costs-which is a frontier in clinical drug research. In the past years, several chromatographic and non-chromatographic alternatives have been explored for this purpose, resulting in the development of efficient platforms for the purification of mAbs, that are overviewed and discussed in this chapter. In summary, this chapter provides a vision on the current state of the art of the biopharmaceuticals market, on the production and use of mAbs as valuable therapeutic agents, including their use for the treatment of infectious diseases, while summarizing the mAbs-based products already approved by regulatory agencies. New insights concerning the development of new and alternative platforms or the extraction

show abstract

Section: Nimentioning

confidence: 99%

Monoclonal Antibodies - Addressing the Challenges on the Manufacturing Processing of an Advanced Class of Therapeutic Agents

Capela¹,

Aires‐Barros²,

Freire³

et al. 2017

Frontiers in Clinical Drug Research: Anti-Infectives Volume 4

View full text Add to dashboard Cite

show abstract

“…A novel chromatography technique incorporating the selectivity of PEG‐induced precipitation was developed by the Gagnon group [92–95]. This technique is referred to as steric exclusion chromatography.…”

Section: Downstream Process Unit Operations For Virus‐like Particlesmentioning

confidence: 99%

Next generation vaccines and vectors: Designing downstream processes for recombinant protein‐based virus‐like particles

Effio

Hubbuch

2015

Biotechnology Journal

View full text Add to dashboard Cite

In recent years, the development of novel recombinant virus-like particles (VLPs) has been generating new perspectives for the prevention of untreated and arising infectious diseases. However, cost-reduction and acceleration of manufacturing processes for VLP-based vaccines or vectors are key challenges for the global health system. In particular, the design of rapid and cost-efficient purification processes is a critical bottleneck. In this review, we describe and evaluate new concepts, development strategies and unit operations for the downstream processing of VLPs. A special focus is placed on purity requirements and current trends, as well as chances and limitations of novel technologies. The discussed methods and case studies demonstrate the advances and remaining challenges in both rational process development and purification tools for large biomolecules. The potential of a new era of VLP-based products is highlighted by the progress of various VLPs in clinical phases.

show abstract

“…Ascites fluids were collected daily, centrifuged at 10,000 g for 10 minutes, and stored in the presence of sodium azide at 4℃. The supernatants of the ascites fluids were purified by the steric exclusion of polyethylene glycol [20]. Then, the crude products were diluted to 1 mg/ml with a binding buffer containing 0.5 mol/L NaCl at pH 7.4 and applied to a protein A agarose column (GE, USA) [21].…”

Section: Preparation and Purification Of The Monoclonal Antibodymentioning

confidence: 99%

A monoclonal antibody targeting the dimer interface of epidermal growth factor receptor (EGFR)

et al. 2016

View full text Add to dashboard Cite

Epidermal growth factor receptor (EGFR) is an attractive target for the treatment of epithelial cancers. However, EGFR antagonists have low clinical response rates and frequently induce resistance mainly caused by the hypermutation of the extracellular and intracellular domains and the heterodimerization of EGFR. Dimerization plays a key role in the activation of the EGFR family of receptors. Thus, targeting the highly conserved dimer interface of EGFR maybe an attractive strategy for improving the clinical response of anti-EGFR therapies. In this work, we report a monoclonal antibody (mAb) called Antidimer 5G9 that targets the β-hairpin within the dimer interface of EGFR, which is 100% homologous with mouse EGFR. Antidimer 5G9 belongs to the isotype IgG1 and bound with an affinity constant of 1.837×10L/mol. Just as designed and expected, Antidimer 5G9 could recognize and bind to human EGFRs or mouse EGFRs on the surface of human breast cancer cells of the MDA-MB-231 cell line or mouse Lewis lung cancer cells (LLC), effectively inhibiting growth and inducing apoptosis in the targeted cells. This work lays the foundation for further studies investigating the feasibility of this strategy for targeting the dimer interface of EGFR and developing novel anti-EGFR drugs.

show abstract

High productivity purification of immunoglobulin G monoclonal antibodies on starch-coated magnetic nanoparticles by steric exclusion of polyethylene glycol

Cited by 42 publications

References 46 publications

Monoclonal Antibodies - Addressing the Challenges on the Manufacturing Processing of an Advanced Class of Therapeutic Agents

Monoclonal Antibodies - Addressing the Challenges on the Manufacturing Processing of an Advanced Class of Therapeutic Agents

Next generation vaccines and vectors: Designing downstream processes for recombinant protein‐based virus‐like particles

A monoclonal antibody targeting the dimer interface of epidermal growth factor receptor (EGFR)

Contact Info

Product

Resources

About