Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells. 1. Behavior of mono- to hexapeptides

Analytical Chemistry
Carolina SimóPier Giorgio Righetti

Abstract

For a better understanding of the behavior of solid-phase combinatorial peptide ligands for capturing the red blood cell low-abundance soluble proteome, combinatorial peptides of different lengths from a single amino acid up to a hexapeptide were evaluated. A red blood cell lysate (6 g total protein) was loaded in a cascade fashion to the six columns, which were individually eluted with 8 M urea, 2% 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (v/w), and 50 mM citric acid. Each eluate was analyzed via sodium dodecyl sulfate polyacrylamide gel electrophoresis, two-dimensional maps, and nanoLC-MS/MS. mixed beads with a single amino acid attached showed the capture of a non-negligible portion of the proteome. A progressive increasing of the length of the peptide bait enlarges the pool of captured proteins. Above a length of four amino acids, a plateau is progressively reached, suggesting that not much could be gained with baits longer than six amino acids. Interestingly, whereas the beads laden with a single amino acid seem to be able to capture large-size proteins (>40 kDa), beads with progressively longer peptides capture additional proteins in the smaller size range (10-50 kDa). This suggests that interactions alre...Continue Reading

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Citations

May 25, 2010·Analytical and Bioanalytical Chemistry·Angelo D'Alessandro, Lello Zolla
Jan 23, 2010·Molecular & Cellular Proteomics : MCP·Emmanuelle Mouton-BarbosaAnne Gonzalez de Peredo
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Jun 9, 2009·Journal of Proteome Research·Alfonsina D'AmatoPier Giorgio Righetti
Aug 2, 2014·Analytical Chemistry·Pier Giorgio RighettiEgisto Boschetti

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