Abstract: A method for modification of solid substrates with proteins for efficient surface preconcentration of an analyte from multi-component samples before the detection based on desorption-ionization mass spectrometry and immunochemical assays. The claimed subject is a method of modification of surfaces used as substrates for desorption-ionization mass spectrometry and immunochemical assays. The method is based on electronebulization (electrospraying) of protein solution, depending on the intended application either enzymes, lectins, or antibodies. The formed charged electrospray is dried in real time by its passing through an evaporation compartment and the resulting beam of desolvated ions impacts onto the surface and binds to it firmly. Such modified surface can be then used for a selective interaction with an affinity partner of the deposited protein, its preconcentration or enzymatic modification followed by an analysis by means of desorption-ionization mass spectrometry or immunochemical assays.

Abstract: The invention relates to the affinity plate for haptoglobin phenotype determination, the kit comprising it, and the method of haptoglobin phenotype determination by detection of its a subunits by means of mass spectrometry desorption ionization techniques after preceding preconcentration of haptoglobin on the surface of the affinity plate with immobilized anti-haptoglobin antibody that was deposited onto this surface from gas phase after preceding electrospray ionization and heat desolvation.

Abstract: A method for modification of solid substrates with proteins for efficient surface preconcentration of an analyte from multi-component samples before the detection based on desorption-ionization mass spectrometry and immunochemical assays. The claimed subject is a method of modification of surfaces used as substrates for desorption-ionization mass spectrometry and immuno-chemical assays. The method is based on electronebulization (electrospraying) of protein solution, depending on the intended application either enzymes, lectins, or antibodies. The formed charged electrospray is dried in real time by its passing through an evaporation compartment and the resulting beam of desolvated ions impacts onto the surface and binds to it firmly. Such modified surface can be then used for a selective interaction with an affinity partner of the deposited protein, its preconcentration or enzymatic modification followed by an analysis by means of desorption-ionization mass spectrometry or immunochemical assays.

Abstract: A method of surface modification for analyzing of phosphorylated peptides. The surface of solid substrates is modified for efficient phosphorylated peptide preconcentration from complex peptide mixtures prior to detection based on desorption/ionization mass spectrometry. The method of surface functionalization is introduced by ambient ion landing. The approach is based on electronebulization, differently said electrospray, of solutions of organometallic compounds related to elements of 4B class of periodic table of elements, especially to zirconium, hafnium and titanium. The generated charged electrospray is dried on the fly by passing the heated compartment and focused to a surface for modification forming a stable oxide layer there. The surface modified this way has been used for phosphopeptide enrichment from peptide mixtures prior to desorption/ionization mass spectrometry.

Abstract: The invention has been based on original way of surface modification of solid substrates for efficient phosphorylated peptide preconcentration from complex peptide mixtures prior to detection based on desorption/ionization mass spectrometry. The subject of protection is the method of surface functionalization by ambient ion landing. The approach was based on electronebulization (electrospray) of solutions of organometallic compounds related to elements of 4B class of periodic table of elements, especially to zirconium, hafnium and titanium. The generated charged electrospray was dried on the fly by passing the heated compartment and focused to a surface forming a stable oxide layer there. The surface modified this way has been used for phosphopeptide enrichment from peptide mixtures prior to desorption/ionization mass spectrometry.