Affinity purification of von Willebrand factor using ligands derived from peptide libraries

Huang, Ping Yu; Baumbach, George A.; Dadd, Christopher A.; Buettner, Joseph A.; Masecar, Barbara L.; Hentsch, Marc; Hammond, David J.; Carbonell, Ruben G.

doi:10.1016/0968-0896(96)00066-1

Cited by 52 publications

(25 citation statements)

References 11 publications

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“…As already reported, a single bead is capable of capturing more than a single species (Huang et al, 1996;Miyamoto et al, 2008) with presumably different association constants. The interaction phenomenon being governed by the mass action law, displacement effects are not only dependent on affinity constants but also on the relative concentration of species having affinity for the same peptide ligand.…”

Section: Citationmentioning

confidence: 66%

“…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%

“…Structurally identified peptides although not identical were quite similar and they generally shared three amino acids. As reported by Huang et al, (1996), about two dozens of peptides were identified for the capture of von Willebrand factor from human plasma. Some peptides released the captured proteins upon sodium chloride wash, others after contact with a solution of acetic acid.…”

Section: Citationmentioning

confidence: 94%

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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: Citationmentioning

confidence: 66%

Section: Resultsmentioning

confidence: 99%

Section: Citationmentioning

confidence: 94%

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Protein Sample Treatment with Peptide Ligand Library: Coverage and Consistency

Li¹,

Sun²,

Freeby³

et al. 2009

J Proteomics Bioinform

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“…This corresponds to a ligand density of 5 to 15 lmol/mL gel. Huang et al [24] reported a ligand density of 32 -60 mg hexapeptide per mL Peptide sequences from the N terminus to the C terminus…”

Section: Affinity Chromatography On Beaded Materials With Selected Canmentioning

confidence: 99%

“…However, they are physically and chemically stable ligands and very resistant against proteolytic cleavage. Furthermore, a site directed immobilization is possible, and a high ligand density can be achieved [23,24]. Further advantages are their low toxicity and their low immunogenicity.…”

Section: Introductionmentioning

confidence: 99%

Affinity Chromatography of Human Blood Coagulation Factor VIII on Monoliths with Peptides from a Combinatorial Library

Amatschek

Necina

Hahn

et al. 2000

J. High Resol. Chromatogr.

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Affinity chromatographic screening of soluble combinatorial peptide libraries

Huang

Carbonell

1999

Biotechnol. Bioeng.

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Affinity chromatography using immobilized S‐protein was used for the screening of affinity peptide ligands from two soluble peptide libraries. Peptide library I consisted of octamers with glycine (G) at both termini of each peptide, i.e. GXXXXXXG. The six center positions were constructed using random sequences of six L‐amino acids (Y, N, F, E, V, and L). Peptide library II also consisted of octamers but with glycine and valine (V) at both termini of each peptide (GVZZZZVG). The four variable center positions of peptide library II were random sequences of 18 L‐amino acids. Peptides that were retained specifically on the immobilized S‐protein column were eluted by 2% acetic acid. The peptides in the acid eluate were further separated using reversed‐phase HPLC. Each separated peptide fraction was collected and the peptide sequences deconvoluted by mass spectrometry (MS/MS). The screenings of peptide libraries I and II resulted in 12 and 7 affinity peptides, respectively. Eight out of the twelve peptides from peptide library I contained the clear consensus sequence NFEV. Peptide library II resulted in affinity peptides with the sequences GVNFEVVG, GVNFTVVG and GVFFEL(I)VG. The advantages and limitations of affinity chromatography in peptide library screening are discussed. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 63: 633–641, 1999.

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Affinity purification of von Willebrand factor using ligands derived from peptide libraries

Cited by 52 publications

References 11 publications

Protein Sample Treatment with Peptide Ligand Library: Coverage and Consistency

Protein Sample Treatment with Peptide Ligand Library: Coverage and Consistency

Affinity Chromatography of Human Blood Coagulation Factor VIII on Monoliths with Peptides from a Combinatorial Library

Affinity chromatographic screening of soluble combinatorial peptide libraries

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