Enzymatic hydrolysis of reconstituted dimyristoylphosphatidylcholine-apo A-I complexes》.pdfVIP

Biochimica et Biophysica Acta, 1151(1993) 137-142 137 © 1993Elsevier Science Publishers B.V. All rights reserved 0005-2736/93/$06.00 BBAMEM 76071 Enzymatic hydrolysis of reconstituted dimyristoylphosphatidylcholine-apo A-I complexes Laurence Lins a, Sandrine Piron a, Karl Conrath b, Berlinda Vanloo c, Robert Brasseur a, Maryvonne Rosseneu c, Johan Baert d and Jean-Marie Ruysschaert a a Laboratoire de Chimie Physique des Macromol~cules aux Interfaces, Free University of Brussels, Brussels (Belgium), b Smith Kline Beecham Biologicals, Chimie des Prot#ines, Rixensart (Belgium), c Department of Clinical Chemistry, Academic Hospital St. Jan, Brugge (Belgium) and d Katholieke Universiteit Leuven, Campus Kortrijk, Interdisciplinary Research Centre, Kortrijk (Belgium) (Received 25 February 1993) Key words: Limited proteolysis; Reconstituted dimyristoylphosphatidylcholine-apo A-I complex; Protein-lipid interaction Apolipoproteins share a common structural feature, their interaction with phospholipids. It is believed that amphipathic helical sequences enable apolipoproteins to bind to lipid bilayer and to form discoidal particles of defined dimensions. While the knowledge of the apo A-I sequence and secondary structure has been used to make predictions about its mode of association with lipids, the available experimental data necessary to propose a precise model of these discoidal structures are still limited. An important step in our understanding of these structur