Purification of proteins using peptide-ELP based affinity precipitation

Mullerpatan, Akshat; Chandra, Divya; Kane, Erin M.; Karande, Pankaj; Cramer, Steven M.

doi:10.1016/j.jbiotec.2019.12.012

Cited by 27 publications

(23 citation statements)

References 30 publications

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“…1,2 There is also growing interest in the use of precipitation for the initial purification (capture) of monoclonal antibody (mAb) products due to the significant increase in product titer that have been achieved over the past two decades. 3,4 mAbs have been successfully precipitated using cold ethanol and CaCl 2, 5 polyethylene glycol (PEG), 6 PEG and CaCl 2, 7 CaCl 2 and caprylic acid, 8 PEG and low pH 9 , zinc chloride (ZnCl 2 ) and PEG, 10 and elastin-like polypeptides (ELP) 11,12 among others.…”

mentioning

confidence: 99%

Enhanced filtration performance usingfeed‐and‐bleedconfiguration for purification of antibody precipitates

Zhao

Chen

Andini

et al. 2020

Biotechnology Progress

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Precipitation can be used for the initial purification of monoclonal antibodies (mAbs), with the soluble host cell proteins removed in the permeate by tangential flow microfiltration. The objective of this study was to examine the use of a feed-andbleed configuration to increase the effective conversion (ratio of permeate to feed flow rates) in the hollow fiber module to enable more effective washing of the precipitate. Experiments were performed using human serum Immunoglobulin G (IgG) precipitates formed with 10 mM zinc chloride and 7 wt% polyethylene glycol. The critical flux was evaluated as a function of the shear rate and IgG concentration, with the resulting correlation used to predict conditions that can achieve 90% conversion in a single pass with minimal fouling. Experimental data for both the start-up and steady-state performance are in good agreement with model calculations. These results were used to analyze the performance of an enhanced continuous precipitation-microfiltration process using the feed-and-bleed configuration for the initial capture / purification of a mAb product.

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mentioning

confidence: 99%

Enhanced filtration performance usingfeed‐and‐bleedconfiguration for purification of antibody precipitates

Zhao

Chen

Andini

et al. 2020

Biotechnology Progress

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“…In these strategies, the use of tandem repeats of the affinity ligand can improve the capture efficiency [103] . The versatility of this approach has also been shown with the successful purification of different proteins [103] , [104] and it may also be considered for immobilization purposes if multiple affinity ligands are used.…”

Section: Protein Purification/immobilization Tagsmentioning

confidence: 99%

“…Both the thermo-responsive ELP and pH-responsive CspB50 reveal to be very attractive tags for non-chromatography-based protein purification methods, being emergent alternatives to conventional matrices [101] , [105] . However, most of the interactions of self-aggregating tags rely on environmental conditions such as temperature, pH and ionic strength, which may not be suited to maintain the activity of the tagged protein [103] , [104] . To overcome these limitations, other types of tags have been recently explored, namely for magnetic-absorption-based purification and immobilization of proteins [97] .…”

Section: Protein Purification/immobilization Tagsmentioning

confidence: 99%

Tag-mediated single-step purification and immobilization of recombinant proteins toward protein-engineered advanced materials

Freitas

Domingues

Aguiar

2022

Journal of Advanced Research

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“…Based on this critical study, ELP‐tagged purification systems, in which ELPs can be fused to the target protein either genetically [ 174 ] or via other linkers, [ 175 ] were developed as an option for purifying thermally stable proteins without incorporation of affinity binding tags and expensive resin. [ 175–177 ]…”

Section: Applications For Idpps With Nanoscale and Microscale Control Enabled By Llpsmentioning

confidence: 99%

Application of Thermoresponsive Intrinsically Disordered Protein Polymers in Nanostructured and Microstructured Materials

Wang

Patkar

Kiick

2021

Macromolecular Bioscience

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Modulation of inter‐ and intramolecular interactions between bioinspired designer molecules can be harnessed for developing functional structures that mimic the complex hierarchical organization of multicomponent assemblies observed in nature. Furthermore, such multistimuli‐responsive molecules offer orthogonal tunability for generating versatile multifunctional platforms via independent biochemical and biophysical cues. In this review, the remarkable physicochemical and mechanical properties of genetically engineered protein polymers derived from intrinsically disordered proteins, specifically elastin and resilin, are discussed. This review highlights emerging technologies which use them as building blocks in the fabrication of highly programmable structured biomaterials for applications in delivery of biotherapeutic cargo and regenerative medicine.

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Purification of proteins using peptide-ELP based affinity precipitation

Cited by 27 publications

References 30 publications

Enhanced filtration performance usingfeed‐and‐bleedconfiguration for purification of antibody precipitates

Enhanced filtration performance usingfeed‐and‐bleedconfiguration for purification of antibody precipitates

Tag-mediated single-step purification and immobilization of recombinant proteins toward protein-engineered advanced materials

Application of Thermoresponsive Intrinsically Disordered Protein Polymers in Nanostructured and Microstructured Materials

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