This thesis reports on the adsorption of two amino acids (AA) with different properties, Leucine and Glutamic acid, on the amorphous silica surface. It exemplifies a general approach to hybrid systems that combines experimental information and molecular modeling in order to characterize at the molecular level the interaction of organic molecules with adsorption sites on the surface of inorganic minerals. State-of-the-art spectroscopic techniques, chiefly IR spectroscopy and solid-state NMR, were used to gather information on the functional groups of the amino acids and the way they were modified by the adsorption. In conjunction with macroscopic characterization techniques such as X-Ray Diffraction (XRD) and Thermogravimetric Analysis (TGA), which allowed the identification of the parameters that govern surface speciation chiefly the activity of water as well as the competition between site adsorption and precipitation as a separate crystal phase. For both amino acids, experimental data indicate that adsorption involves the formation of specific H-bonds with groups of surface silanols. DFT modeling showed that stable H-bonded adducts can indeed be formed involving silanols, one amino acid molecule and several molecules of water – anhydrous models did not correspond to the experimental observations, especially regarding the observed prevalence of zwitterions. Theoretical values of NMR chemical shifts were calculated and corresponded quite well with the experimental values, once again favouring microsolvated models. Amide formation occurred at moderate temperatures. When adsorbed alone, Glu mostly converted to the cyclic form, pyroGlutamic acid, while Leu was mostly transformed to the cyclic dimer, cyclo(Leu-Leu). Both forms may be considered as “dead ends”. In contrast, when they were adsorbed together on the silica surface, they gave rise to the formation of linear oligopeptides that may be considered as a first step towards the emergence of proteins.