title: Combinatorial ligand libraries as a two-dimensional method for proteome analysis.
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 (25mM NaCl) or at high concentrations of lyotropic salts of the Hofmeister series (1M 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.
authors.affiliation: Nephrology, Dialysis, Transplantation Unit and Laboratory on Pathophysiology of Uremia, Istituto Giannina Gaslini, 16148 Genoa, Italy.
authors.forename: Laura
authors.initials: L
authors.lastname: Santucci
authors.forename: Giovanni
authors.initials: G
authors.lastname: Candiano
authors.forename: Andrea
authors.initials: A
authors.lastname: Petretto
authors.forename: Chiara
authors.initials: C
authors.lastname: Lavarello
authors.forename: Maurizio
authors.initials: M
authors.lastname: Bruschi
authors.forename: Gian Marco
authors.initials: GM
authors.lastname: Ghiggeri
authors.forename: Attilio
authors.initials: A
authors.lastname: Citterio
authors.forename: Pier Giorgio
authors.initials: PG
authors.lastname: Righetti
mesh_terms: D001798:Blood Proteins / Q000032:analysis / Q000737:chemistry; D002846:Chromatography, Affinity; D020650:Combinatorial Chemistry Techniques / Q000379:methods*; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D013058:Mass Spectrometry; D017711:Nonlinear Dynamics; D009994:Osmolar Concentration; D019151:Peptide Library; D020543:Proteome / Q000032:analysis* / Q000737:chemistry; D040901:Proteomics / Q000379:methods*
chemical_list: D001798:Blood Proteins; D019151:Peptide Library; D020543:Proteome