Novel ligands for the affinity-chromatographic purification of antibodies

Fassina, Giorgio; Ruvo, Menotti; Palombo, Giovanna; Verdoliva, Antonio; Marino, Maria

doi:10.1016/s0165-022x(01)00215-9

Cited by 124 publications

(95 citation statements)

References 47 publications

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“…This technique is not only used for the purification of immunoglobulins but is also widely applied in the manufacture and detection of pesticides, drugs, and hormones. However, despite the obvious advantages, immuno-affinity chromatography has some unfortunate disadvantages, like degradation or leaching of ligands, which consequently raise costs [FASSINA, et al 2001, JOHNSON 1986, STEVENSON 2000, SUBRAMANIAN 2002.…”

Section: Traditional Methods For Immunoglobulin Enrichmentmentioning

confidence: 99%

Enrichment behavior of immunoglobulin by foam fractionation using response surface methodology

Chen

Parlar

2013

Separation and Purification Technology

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Section: Traditional Methods For Immunoglobulin Enrichmentmentioning

confidence: 99%

Enrichment behavior of immunoglobulin by foam fractionation using response surface methodology

Chen

Parlar

2013

Separation and Purification Technology

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“…To overcome the disadvantages, several synthetic ligands have been proposed as replacements for protein A in the affinity purification of antibodies; these include the use of a thiophilic ligand (Porath et al 1985), histidyl ligand (Elkak and Vjiayalakshmi 1991), Avid A1 (Ngo and Khatter 1990), or peptides or nonpeptides designed to mimic protein A (Fassina et al 2001; for review, see Huse et al 2002). However, to our knowledge none of these have as yet become protein A alternatives at the manufacturing level.…”

Section: Introductionmentioning

confidence: 99%

Structural and molecular basis for hyperspecificity of RNA aptamer to human immunoglobulin G

Miyakawa¹,

Nomura²,

Sakamoto³

et al. 2008

RNA

109

107

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Potential applications for functional RNAs are rapidly expanding, not only to address functions based on primary nucleotide sequences, but also by RNA aptamer, which can suppress the activity of any target molecule. Aptamers are short DNA or RNA folded molecules that can be selected in vitro on the basis of their high affinity for a target molecule. Here, we demonstrate the ability of RNA aptamers to recognize-and bind to-human IgG with high specificity and affinity. An optimized 23-nucleotide aptamer, Apt8-2, was prepared, and was shown to bind to the Fc domain of human IgG, but not to other IgG's, with high affinity. Apt8-2 was observed to compete with protein A, but not with the Fcg receptor, for IgG binding. NMR chemical-shift analyses localized the aptamer-binding sites on the Fc subdomain, which partially overlaps the protein A binding site but not the Fcg receptor binding site. The tertiary structures of the predicted recognition sites on the Fc domain differ significantly between human IgG and other species of IgGs; this, in part, accounts for the high specificity of the selected aptamer. Apt8-2 can therefore be used as a protein A alternative for affinity purification of human IgG and therapeutic antibodies. Using Apt8-2 would have several potential advantages, raising the possibility of developing new applications based on aptamer design.

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“…Towards this, a tripeptide tetramer ((Arg-Thr-Tyr)4-Lys2-Lys-Gly) has been described that binds to the Fc portion of IgG (Fassina et al 2001) and yields approximately 95% pure protein. It also demonstrates a broad range of specificities for antibodies from a variety of hosts (i.e.…”

Section: Synthetic Peptidesmentioning

confidence: 99%

“…Support Reference ((Arg-Thr-Tyr)4-Lys2-Lys-Gly IgG Sepharose (Fassina et al 2001) Asp-Ala-Ala-Gly IgG Agarose (Lund et al 2012) His-Trp-Arg-Gly-TrpVal IgG Toyopearl amino-650M resin (Menegatti et al 2012) His-Trp-Arg-Gly-TrpVal * Human IgG Toyopearl amino-650M resin (Yang et al 2009 Phe-Leu-Leu-Val-ProLeu Fibrinogen Toyopearl amino-650M resin (Kaufman et al 2002) (Gly-Ala-Met-His-LeuPro-Trp-His-Met-GlyThr-Leu)4…”

Section: Peptide Sequencementioning

confidence: 99%

Advances in affinity ligand‐functionalized nanomaterials for biomagnetic separation

Fields

O'Mahony

et al. 2015

Biotech & Bioengineering

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The downstream processing of proteins remains the most significant cost in protein production, and is largely attributed to rigorous chromatographic purification protocols, where the stringency of purity for biopharmaceutical products sometimes exceeds 99%. With an ever burgeoning biotechnology market, there is a constant demand for alternative purification methodologies, to ameliorate the dependence on chromatography, while still adhering to regulatory concerns over product purity and safety. In this article, we present an up-to-date view of bioseparation, with emphasis on magnetic separation and its potential application in the field. Additionally, we discuss the economic and performance benefits of synthetic ligands, in the form of peptides and miniaturized antibody fragments, compared to full-length antibodies. We propose that adoption of synthetic affinity ligands coupled with magnetic adsorbents, will play an important role in enabling sustainable bioprocessing in the future.

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Novel ligands for the affinity-chromatographic purification of antibodies

Cited by 124 publications

References 47 publications

Enrichment behavior of immunoglobulin by foam fractionation using response surface methodology

Enrichment behavior of immunoglobulin by foam fractionation using response surface methodology

Structural and molecular basis for hyperspecificity of RNA aptamer to human immunoglobulin G

Advances in affinity ligand‐functionalized nanomaterials for biomagnetic separation

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