Migration of optical excited states of the modified chromium complexes of collagen

Abstract

Photoluminescent properties of the collagen modified by chrome complexes are investigated. The analysis of the spectra of a photoluminescence at excitation in ultra-violet area shows that intrinsic photoluminescence of collagen undergoes a quenching with the increase of content of chromic complexes. In the modified collagen luminescence ranges are also deformed with full quenching of phenylalanine peak. The kinetics of decay of a photoluminescence of samples of the native and modified collagen, samples of phenylalanine and a tyrosine is measured. With the increase of content of chrome complexes in the modified collagen there is a redistribution of the dominating role of the radiating centers of collagen from the phenylalanine residue to tyrosine residue.