The structural stability of low-density lipoprotein. A kinetic X-ray scattering study of its interaction with arterial proteoglycans.

The structural stability of human plasma low-density lipoproteins (LDL) has been studied kinetically by means of dynamic X-ray scattering techniques. At 37 degrees C, rapid deterioration of the lipoproteins present in the insoluble complex which is formed on mixing solutions of LDL and human arterial proteoglycans is observed. This is evidenced by the progressive blurring of the X-ray scattering spectra. At 4 degrees C the X-ray patterns from the insoluble complex show a single reflection centered at 34 A-1, which is characteristic of pure cholesteryl esters organized in a smectic phase. This behaviour contrasted with the high stability exhibited by free LDL at 37 degrees C. Our results show that, in the form of insoluble complex, the lipoprotein molecules are rapidly disrupted and that the neutral lipids segregated with formation of a lipid phase. This suggests that LDL particles become destabilized by their interaction with arterial proteoglycans.