Isolation of a peptide ligand for affinity purification of factor VIII using phage display

Kelley, Brian; Booth, James A.; Tannatt, Molly; Wu, Qilong; Ladner, Robert C.; Yu, Jinan; Potter, Daniel; Ley, Arthur C.

doi:10.1016/j.chroma.2004.03.041

Cited by 36 publications

(26 citation statements)

References 14 publications

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“…Combinatorially generated peptides specific for plasma proteins have been used to selectively capture plasma ligands [31]. Peptides from these libraries can have affinities in the nanomolar range with high specificity [32,33].…”

Section: Resultsmentioning

confidence: 99%

Depletion and fractionation technologies in plasma proteomic analysis

Tam

Pirro

Hinerfeld

2004

Expert Review of Proteomics

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This review intends to survey the traditional and current technologies in the depletion and subfractionation of plasma proteins for further analyses. The value of depletion aims to enrich low-abundant proteins by removing highly abundant proteins, such as albumin or immunoglobulin G, from plasma. With this approach, one can examine both the resulting high- and low-abundant protein fractions. The depleted protein population can be further subfractionated based on their isoelectric point ranges, creating a more discrete pool of proteins for detailed post-translational modification studies by methods such as 2D gel electrophoresis and mass spectrometry. The concept of divide to conquer will greatly enhance our ability to identify and characterize low-abundant proteins and cleaved peptides from plasma as important diagnostic markers or potential drug targets. This can potentially reverse the decline in the development of new plasma diagnostic tests.

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Section: Resultsmentioning

confidence: 99%

Depletion and fractionation technologies in plasma proteomic analysis

Tam

Pirro

Hinerfeld

2004

Expert Review of Proteomics

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“…However, when this disulfide constrained heptapeptide was displayed at the gpIII protein coat of M13 filamentous phage, it was demonstrated that M13 phages bearing this particular disulfide constrained heptapeptide formed a tighter binding with truncated HBcAg compared with free cyclic peptide bearing the same sequence as well as phages bearing the sequence LLGRMK [18]. Spontaneous disulfide bonds would form and the displayed peptides would gain a defined conformation, which subsequently altered the properties of the displayed residues, different from how they exist as free peptide or in linear forms [18,29]. In addition, it has been described that most of the peptide ligand would only function when they are an integral part of the phage coat protein [30].…”

Section: Calculationsmentioning

confidence: 96%

Purification of recombinant hepatitis B core antigen from unclarified Escherichia coli feedstock using phage-immobilized expanded bed adsorption chromatography

Tan

Tey

2012

Journal of Chromatography B

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“…As a result, the clones bound to proteins with artificial conformations when antigens were immobilized on a solid matrix were avoided (16). Although phage library-derived ligands were extensively studied (23,25,26), employing phage particles directly as affinity ligands was a relatively new concept. In the present work, phage-displayed scFv fragments were cross-linked to serve as affinity matrices for a favorable alternative, compared with phage-displayed peptides or wild-type phages as reported before (14,19,27).…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, many efforts are aimed at applying phage Phage applied (pfu) 1.6 ϫ 10 library for ligand identification (23,24). However, strategies of panning on a complex antigen system were always under studies in contrast to ligand screening against one individual antigen.…”

Section: Discussionmentioning

confidence: 99%

A Novel Strategy for Proteome-wide Ligand Screening Using Cross-linked Phage Matrices

Qian

Liu

Tang

et al. 2010

Journal of Biological Chemistry

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To find a suitable ligand from a complex antigen system is still a mission to be accomplished. Here we have explored a novel "library against proteome" panning strategy for ligand screening and antigen purification from a complex system using phage-displayed antibody technology. Human plasma proteome was targeted for phage library panning. During the process, the panning was carried out in solution, using a biotin/ streptavidin beads separation system, for three rounds. Nine monoclonal phages, bound tightly to a number of unknown plasma proteins, were selected from the last round, six of which were directly employed as cross-linked matrices to purify their corresponding antigens from the plasma. The proteins isolated by G5 and E1 matrices were identified as amyloid protein and apolipoprotein A-I precursor, respectively. The results demonstrated that it was feasible to simultaneously obtain a number of ligand phages for various antigens, including low abundant proteins in a non-comparative proteome-wide system.

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Isolation of a peptide ligand for affinity purification of factor VIII using phage display

Cited by 36 publications

References 14 publications

Depletion and fractionation technologies in plasma proteomic analysis

Depletion and fractionation technologies in plasma proteomic analysis

Purification of recombinant hepatitis B core antigen from unclarified Escherichia coli feedstock using phage-immobilized expanded bed adsorption chromatography

A Novel Strategy for Proteome-wide Ligand Screening Using Cross-linked Phage Matrices

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