Combinatorial ligand libraries as a two-dimensional method for proteome analysis

Laura Santucci, Giovanni Candiano, Andrea Petretto, Chiara Lavarello, Maurizio Bruschi, Gian Marco Ghiggeri, Attilio Citterio, Pier Giorgio Righetti

Research output: Contribution to journalArticlepeer-review

Abstract

The present report tries to assess the possibility of performing capture of proteomes via combinatorial peptide ligand libraries (CPLL) in a two-dimensional (2D) mode, i.e. via orthogonal complementarity in the capture phase. To that aim, serum proteins are captured at physiological pH either at low ionic strength (25. mM NaCl) or at high concentrations of lyotropic salts of the Hofmeister series (1. M ammonium sulphate) favouring hydrophobic interaction. Indeed such 2D mechanisms seems to be operative, since 52% of the captured proteins are common to the two capture modes, 20% are specific only of the "ionic" interaction mode and 28% are found only in the "hydrophobically" driven interaction. As an additional bonus, losses of protein species from the initial sample, one of the major drawbacks of CPLLs, are diminished to about 5% and are found only in the ionic capture, whereas the hydrophobically engendered capture is loss-free.

Original languageEnglish
Pages (from-to)106-112
Number of pages7
JournalJournal of Chromatography A
Volume1297
DOIs
Publication statusPublished - Jul 5 2013

Keywords

  • Combinatorial peptide ligand libraries
  • Human serum
  • Hydrophobic capture
  • Ionic capture
  • Mass spectrometry

ASJC Scopus subject areas

  • Analytical Chemistry
  • Organic Chemistry
  • Biochemistry

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