Influence of C-terminal α-helix hydrophobicity and aromatic amino acid content on apolipoprotein A-I functionality》.pdfVIP

Biochimica et Biophysica Acta 1821 (2012) 456–463 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal h omepage: www. elsevi /locate/bbali p Influence of C-terminal α-helix hydrophobicity and aromatic amino acid content on ☆ apolipoprotein A-I functionality Nicholas N. Lyssenko a, Mami Hata b, Padmaja Dhanasekaran a, Margaret Nickel a, David Nguyen a, Palaniappan Sevugan Chetty a, Hiroyuki Saito b, Sissel Lund-Katz a, Michael C. Phillips a,⁎ a Lipid Research Group, Gastroenterology, Hepatology and Nutrition Division, Childrens Hospital of Philadelphia, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-4318, USA b Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima, Tokushima 770-8505, Japan a r t i c l e i n f o a b s t r a c t Article history: The apoA-I molecule adopts a two-domain tertiary structure and the properties of these domains modulate Received 31 March 2011 the ability to form HDL particles. Thus, human apoA-I differs from mouse apoA-I in that it can form smaller Received in revised form 30 June 2011 HDL particles; the C-terminal α-helix is important in this process and human apoA-I is unusual in containing Accepted 29 July 2011 aromatic amino acids in the non-polar face of this amphipathic α-helix. To understand the influence of these Available online 5 August 2011 aromatic amino acids