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The biocompatibility evaluation of aluminosilicate samples containing iron and dysprosium or yttrium was made with respect to collagen (type I from calf skin) adsorption. The SEM analysis indicates morphological changes on samples surface after incubation in collagen solution. At the same time, the features of ATR-FTIR spectra and the data obtained by deconvolution of the amide I region of adsorbed collagen show qualitative and quantitative diferences compared to the native protein. The secondary structure of collagen is more pronounced modified upon adsorption to yttrium aluminosilicate indicating a lower biocompatibility compared to dysprosium containing sample. Cyclic voltammetry also supports the quantitative investigations by collagen adsorption at the Ag/AgCl electrode surface. The current intensity enhancement and the decrease of the oxidation potential of collagen indicate that collagen adsorption is an irreversible process.