Protein Sample Treatment with Peptide Ligand Library: Coverage and Consistency |
Lei Li1, ChengJun Sun1, Steve Freeby1, Dennis Yee1, Sylvie Kieffer-Jaquinod2,
Luc Guerrier3, Egisto Boschetti3*, Lee Lomas1 |
| 1Bio-Rad Laboratories, Hercules, CA 94547, USA |
| 2DSV/IRTSV Laboratoire EdyP, CEA, 38054 Grenoble, France |
| 3Bio-Rad Laboratories, 92430 Marnes-la-Coquette, France |
| *Corresponding author: |
Dr. Egisto Boschetti, Bio-Rad Laboratories, 92430
Marnes-la-Coquette, France,
E-mail: Egisto.boschetti@bio-rad.com |
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| Received November 08, 2009; Accepted December 17, 2009; Published
December 18, 2009 |
| Citation: Li L, Sun C, Freeby S, Yee D, Kieffer-Jaquinod S, et al. (2009)
Protein Sample Treatment with Peptide Ligand Library: Coverage and
Consistency. J Proteomics Bioinform 2: 485-094. doi:10.4172/jpb.1000110 |
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| Copyright: © 2009 Li L, et al. This is an open-access article distributed
under the terms of the Creative Commons Attribution License, which
permits unrestricted use, distribution, and reproduction in any medium,
provided the original author and source are credited. |
| |
| Abstract |
| 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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