[Interaction of apolipoprotein A1 with phospholipids and structure of mixed micelles]

¹Institute of Experimental Cardiology, Russian Cardiological Research and Production Complex, Moscow, Russia.

|October 24, 1998

Abstract:

The structural features of apolipoprotein A1 (apoA1) that provide for the formation of its stable micellar complexes with phosphatidylcholine are discussed. The results of studies on the secondary structure and functional properties of separate sites of the apoA1 polypeptide chain are analyzed. The preparation procedures for discoidal micellar complexes of apoA1 with phosphatidylcholine are discussed, and the characteristics of the complexes are described. The surface activity of apoA1 incorporated into the micellar complexes is characterized, and the recombination mechanisms of lipid-protein micelles in model systems are discussed. The data discussed indicate that all currently known structural-functional properties of apoA1 and its involvement in metabolic and physiological processes are completely determined by the surface activity of the amphiphilic fragments of its conformationally labile polypeptide chain.

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