Abstract
The interaction of meso-tetra-([Formula: see text]-methyl-3-pyridyl)bacteriochlorin tetra 4-methylbenzenesulfonate, meso-tetra-([Formula: see text]-methyl-4-pyridyl)porphine tetraiodide and meso-tetra-([Formula: see text]-methyl-3-pyridyl)porphine tetraiodide with protein was studied. The localization of macrocycles in the protein and their influence on the processes of protein aggregation were established. The aggregation process is initiated by the transition of alpha structures into beta folds, caused by the binding of porphyrins at the sites of protein IB and IIA. The complexes were irradiated with blue and green light. The data obtained showed that by varying the intensity of the light exposure, one can influence the shift of the aggregation equilibrium, obtaining predominantly monomeric or aggregated structures. Thus, photoexposure can be used as an alternative method of treating diseases caused by amyloidosis and for regulating the state of the protein in the pharmacological preparations.
Published Version
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