Elastin--proteoglycan interaction. Conformational changes of alpha-elastin induced by the interaction.

The interaction between alpha-elastin and a connective tissue proteoglycan was followed by optical density measurements and circular dichroism spectroscopy. It was found that interaction takes place at pH values below the isoelectric point of elastin with the formation of a complex coacervate. CD spectra demonstrated conformational changes of alpha-elastin caused by the interaction and resulting in an increase in the content of helical structure. This finding suggests the possibility of the involvement of proteoglycans in the molecular organization of elastin.