Purification of human immunoglobulin G via Fc-specific small peptide ligand affinity chromatography

Yang, Hong; Gurgel, Patrick V.; Carbonell, Ruben G.

doi:10.1016/j.chroma.2008.12.004

Cited by 128 publications

(101 citation statements)

References 32 publications

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“…Investigations performed on influencing factors such as acetylation of the ligand, its density on the resin, and temperature, supported the impression that this ligand is probably the preferred candidate for large-scale affinity separation against current best performing resins (Yang et al, 2009). Encouraged by these data, the investigation was pushed for a better understanding of the performance and docking mechanism (Yang et al, 2010), where the interaction with the Fc portion of IgG was confirmed.…”

Section: Examples Of Successful Affinity Peptide Ligands Discoverymentioning

confidence: 91%

Other Applications of Combinatorial Peptide Libraries

Righetti¹,

Boschetti

2013

Low-Abundance Proteome Discovery

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Section: Examples Of Successful Affinity Peptide Ligands Discoverymentioning

confidence: 91%

Other Applications of Combinatorial Peptide Libraries

Righetti¹,

Boschetti

2013

Low-Abundance Proteome Discovery

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“…The present investigation along with previous work (Yang et al, 2009) Figure 2: SDS-PAGE (4-12%) analysis of whey sample loading experiments set 2. L1: protein ladder; L2: initial whey (1X); L3-6: elution fractions of acid whey sample loading (10 mL) at buffer conductivity of 84 mS.cm -1 ; L7: initial whey (5X); L8-10: elution fractions of IgG spiked (5 mg.mL -1 ) whey sample (1 mL) loading at buffer conductivity of 84 mS.cm -1 ; L11-14: elution fractions of acid whey sample (10 mL) loading at buffer conductivity of 160 mS.cm -1 .…”

Section: Discussionmentioning

confidence: 99%

“…Most of the IgA (>90%) present in the sample was bound to the column with only minor leakage in flow through and bound IgA could be recovered (>95%) in elution with 0.2 M sodium acetate buffer, pH 4.0 ( 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 19 previous investigations related to hexamer peptide interactions with all classes of human Igs (Haiou, 2008;Liu et al, 2012;Menegatti et al, 2012;Yang et al, 2009) and current results with bovine Igs (IgG and IgA) together provide evidence of their capability to extract various classes of Igs from milk (present results) and complex fluids (Haiou, 2008;Yang et al, 2005).…”

Section: Peptide Interactions Towards Bovine Igamentioning

confidence: 99%

“…For example, PAM peptide TG19318 (Fassina et al, 1998), a tetrameric peptide ligand, was successfully investigated for the isolation of various classes of human Igs (IgG, IgA, IgE, IgM) (Huse et al, 2002) from human serum and bacterial cell culture broths. Short linear hexameric peptide ligands HWRGWV, HYFKFD and HFRRHL 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 4 were identified and developed by Carbonell's group through screening of combinatorial libraries on a solid resin and its selectivity towards human Igs through the Fc region was characterised (Yang et al, 2005(Yang et al, , 2009. Unlike protein A/G ligands, these hexameric peptides have a binding spectrum for all subclasses of human Igs (hIgG, IgD, IgE, IgM and, to a lesser extent, IgA) (Liu et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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Application of peptide chromatography for the isolation of antibodies from bovine skim milk, acid whey and colostrum

Billakanti

Fee

Naik

et al. 2014

Food and Bioproducts Processing

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Protein A mimetic peptide ligands have several benefits over conventional Protein A/G ligands, namely that they are small in size, have low production costs, are stable over a wide range of pH values and can withstand cleaning by harsh sanitization agents such as sodium hydroxide. In this paper, a hexamer peptide (HWRGWV) affinity matrix was used for the isolation of bovine immunoglobulins from various dairy streams (skim milk, acid whey and colostrum). Bound immunoglobulins were recovered in elution buffer (0.2 M sodium acetate buffer, pH 4.0) fractions with a purity of >85% in a single step. The peptide resin has achieved a maximum equilibrium adsorption capacity of 23±0.58 mg.mL-1 of resin for bovine IgG and had a dynamic binding capacity of 11.8±0.03 mg.mL-1 at residence time of 2 min. These results suggest that the hexamer peptide chromatography could potentially be used for the selective purification of bovine immunoglobulins from dairy streams. This method has promise as an alternative to conventional Protein A/G chromatography for direct capture of immunoglobulins from streams containing relatively high immunoglobulin concentrations such as colostrum, transgenic or hyper-immune milk. In the abstract, equilibrium adsorption capacity should appear with the associated error (in the previous submission this error appear).Decision: Authors are accepted the above and reviewed as suggested (23±0.58). Comment2.Page 12 line 10 "However, for experiments with standard bIgG at 1 mg mL-1 and 9 mg mL-1 were overloaded" The idea to answer comment 8, reviewer 1 is there but the sentence should better introduced in the text.Decision: Authors are accepted the above and reviewed as suggested in the draft. "However, for experiments with standard bIgG at 1 mg.mL -1 and 9 mg.mL -1 were overloaded since column reached its dynamic capacity approximately at 5.5 mL for 1 mg.mL -1 bIgG and 1.4 mL for 9 mg.mL -1 bIgG. Due to this, % of IgG bound data presented in table 1.1 for these experiments may not reflect the actual numbers". Thank you.Yours sincerely, Jagan M Billakanti, PhD. Cover LetterRevision 2 Reviewer #1 Comment1. In the abstract, equilibrium adsorption capacity should appear with the associated error (in the previous submission this error appear).Decision: Authors are accepted the above and reviewed as suggested (23±0.58) Comment2. Page 12 line 10 "However, for experiments with standard bIgG at 1 mg mL-1 and 9 mg mL-1 were overloaded" The idea to answer comment 8, reviewer 1 is there but the sentence should better introduced in the text.Decision: Authors are accepted the above and reviewed as suggested in the draft."However, for experiments with standard bIgG at 1 mg.mL -1 and 9 mg.mL -1 were overloaded since column reached its dynamic capacity approximately at 5.5 mL for 1 mg.mL -1 bIgG and 1.4 mL for 9 mg.mL -1 bIgG. Due to this, % of IgG bound data presented in table 1.1 for these experiments may not reflect the actual numbers". Detailed Response to ReviewersHighlights  HWRGWV peptide resin showed an equ...

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“…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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Purification of human immunoglobulin G via Fc-specific small peptide ligand affinity chromatography

Cited by 128 publications

References 32 publications

Other Applications of Combinatorial Peptide Libraries

Other Applications of Combinatorial Peptide Libraries

Application of peptide chromatography for the isolation of antibodies from bovine skim milk, acid whey and colostrum

Advances in affinity ligand‐functionalized nanomaterials for biomagnetic separation

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