The binding of proteins on solid surfaces represents an unavoidable step in protein bio-devices production. It can be achieved as reversible (physisorption) or irreversible (chemisorption) binding via covalent bonds between surface groups of the solids and proteins. The latter has the advantage due to the longevity of the surface layer, but often tertiary structure of the protein is disrupted because of which proteins lose their activity. For achieving of the covalent binding of the protein to the surface groups, cross-linking molecules are most often used. Their selection is based on the type of the chemical groups on the solid surface and amino acid residues on the outer surface of the protein. For chemical modification of glass, with silanol groups on the surface, organosilanes are most often used. These are molecules featured with silane groups on the one end which allow condensation with silanol groups at the glass surface, and a terminal functional group on the other end which allows creation of a covalent bond with the target molecule. In the next steps the terminal group of surface-bound organosilanes is converted to a chemical group that can react with some of the amino acid residues of the protein. The reach of the surface reactions is limited by the geometrical influence of the surface on diffusion, as well as other physico-chemical properties of solvated reactants and the surface (primarily liophilicity and surface charge). Therefore, in order to achieve the bonding of the precursors and binding of proteins on the surface, optimization of the physico-chemical conditions for the involved reactions (pH, ionic strength, auxiliary solvent etc.) is required. Since the standard analytical techniques are most often not suitable for the chemical analysis of the surface, due to relatively low concentrations of the analyte, during the development of successful and reproducible methods for protein binding, changes in physico-chemical properties that accompany variation in chemical composition have to be measured for the detection of binding. The aim is to establish an assemblage of analytical methods which can be used as unequivocal proof of protein binding, as well as individual precursors on the surface of borosilicate glass. For surface hydrophobicity measurements, sessile drop contact angle measurements were used, zeta-potential measurements were utilized for the analysis of surface charge, while the X-ray photoelectron spectroscopy was employed for the analysis of elemental composition. This allowed successful assessment of the methods and protocols necessary for chemical modification of the borosilicate glass surface for protein binding, and accomplishment all of the thesis goals.