Affinity purification of fibrinogen using a ligand from a peptide library

Kaufman, Deborah B.; Hentsch, Marc; Baumbach, George A.; Buettner, Joseph A.; Dadd, Christopher A.; Huang, Ping Yu; Hammond, David J.; Carbonell, Ruben G.

doi:10.1002/bit.10120

Cited by 83 publications

(44 citation statements)

References 22 publications

(23 reference statements)

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“…In spite of this "small" volume of beads the experimental data have always been observed to be reproducible. To counterbalance this assessment, it has been several times demonstrated that a given protein can easily be captured by various peptide structures (Huang et al, 1996;Kaufman et al, 2002) and also that a single peptide structure (single bead) can easily capture various species .…”

Section: Resultsmentioning

confidence: 99%

“…This phenomenon was described when elucidating the influence of peptide length on protein capture , on one hand, and more recently when reporting protein patterns when the interaction was performed at different pHs ), on the other hand. Similar peptide libraries were described also as a source of affinity ligands for protein purification with impressive results for a number of proteins (Bastek et al, 2000;Kaufman et al, 2002;Yang et al, 2005). For a given protein more than one single peptide was systematically identified with different adsorption-desorption properties.…”

Section: Citationmentioning

confidence: 99%

See 1 more Smart Citation

Protein Sample Treatment with Peptide Ligand Library: Coverage and Consistency

Li¹,

Sun²,

Freeby³

et al. 2009

J Proteomics Bioinform

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Low-abundance protein detection in biological samples is one of the main challenges in proteomics investigations. One approach that makes the detection of rare species possible is the treatment of biological samples with solidphase combinatorial peptide ligand libraries. However, the use of combinations of ligands opens an uncertainty in that, since the diversity of the library is very large, aliquots of beads sampled from the library might not have fully comparable bead species each time. Reproducibility of experimental data with highly diverse libraries is therefore a main concern to address. This paper reports reproducibility data when aliquots of similar and different volumes of libraries are used at a certain sample to library ratio. Eluates from ligand libraries and other fractions are analyzed using various complementary methods such as two-dimensional gel electrophoresis, immunoassay and mass spectrometry.The collected data show a high level of consistency from sample to sample when processed with similar and variable bead volumes. Analytical determinations are all convergent with each other in considering the similarity of results. It is anticipated that this demonstration reinforces the possibility that differential proteomics studies, in particular for the discovery of protein targets of interest, can effectively be accomplished with combinatorial peptide libraries.

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Section: Resultsmentioning

confidence: 99%

Section: Citationmentioning

confidence: 99%

Protein Sample Treatment with Peptide Ligand Library: Coverage and Consistency

Li¹,

Sun²,

Freeby³

et al. 2009

J Proteomics Bioinform

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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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“…Affinity peptides can be thought of as intermediate between these two cases, as they offer the potential for enormous diversity in chemical properties, and hence selectivity. Further, by using combinatorial methods based on either biological or chemical systems to generate large libraries of unique peptides (Buettner et al, 1996;Kaufman et al, 2002;Ladner, 1995;Sato et al, 2002), sequences may be identified with moderate binding affinities that are sufficient to capture the product without undue losses, but which are still capable of eluting the bound protein under mild conditions.…”

Section: Introductionmentioning

confidence: 99%

Development and validation of an affinity chromatography step using a peptide ligand for cGMP production of factor VIII

Kelley¹,

Tannatt²,

Magnusson

et al. 2004

Biotech & Bioengineering

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An affinity chromatography step was developed for purification of recombinant B-Domain Deleted Factor VIII (BDDrFVIII) using a peptide ligand selected from a phage display library. The peptide library had variegated residues, contained both within a disulfide bond-constrained ring and flanking the ring. The peptide ligand binds to BDDrFVIII with a dissociation constant of f1 AM both in free solution and when immobilized on a chromatographic resin. The peptide is chemically synthesized and the affinity resin is produced by coupling the peptide to an agarose matrix preactivated with N-hydroxysuccinimide. Coupling conditions were optimized to give consistent and complete ligand incorporation and validated with a robustness study that tested various combinations of processing limits. The peptide affinity chromatographic operation employs conditions very similar to an immunoaffinity chromatography step currently in use for BDDrFVIII manufacture. The process step provides excellent recovery of BDDrFVIII from a complex feed stream and reduces host cell protein and DNA by 3 -4 logs. Process validation studies established resin reuse over 26 cycles without changes in product recovery or purity. A robustness study using a factorial design was performed and showed that the step was insensitive to small changes in process conditions that represent normal variation in commercial manufacturing. A scaled-down model of the process step was qualified and used for virus removal studies. A validation package addressing the safety of the leached peptide included leaching rate measurements under process conditions, testing of peptide levels in product pools, demonstration of robust removal downstream by spiking studies, end product testing, and toxicological profiling of the ligand. The peptide ligand affinity step was scaled up for cGMP production of BDDrFVIII for clinical trials. B 2004 Wiley Periodicals, Inc.

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Affinity purification of fibrinogen using a ligand from a peptide library

Cited by 83 publications

References 22 publications

Protein Sample Treatment with Peptide Ligand Library: Coverage and Consistency

Protein Sample Treatment with Peptide Ligand Library: Coverage and Consistency

Advances in affinity ligand‐functionalized nanomaterials for biomagnetic separation

Development and validation of an affinity chromatography step using a peptide ligand for cGMP production of factor VIII

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