Effect of amino acid distribution of amphipathic helical peptide derived from human apolipoprotein A-I on membrane curvature sensing》.pdfVIP

FEBS Letters 587 (2013) 510–515 journal homepage: www.FEBSL Effect of amino acid distribution of amphipathic helical peptide derived from human apolipoprotein A-I on membrane curvature sensing Masafumi Tanaka a,⇑, Yuki Takamura a, Toru Kawakami b, Saburo Aimoto b, Hiroyuki Saito c, Takahiro Mukai a a Department of Biophysical Chemistry, Kobe Pharmaceutical University, Kobe 658-8558, Japan b Laboratory of Protein Organic Chemistry, Institute for Protein Research, Osaka University, Suita 565-0871, Japan c 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: Amphipathic helix, which senses membrane curvature, is of growing interest. Here we explore the Received 30 November 2012 effect of amino acid distribution of amphipathic helical peptide derived from the C-terminal region Revised 8 January 2013 (residues 220–241) of human apolipoprotein (apo) A-I on membrane curvature sensing. This peptide Accepted 11 January 2013 preferred a curved membrane in a manner similar to full-length apoA-I, although its model peptide Available online 21 January 2013 did not sense membrane curvature. Substitution of several residues both on the polar and non-polar Edited by Noboru Mizushima faces of the amphipathic helix had no significant effect on sensing, suggestive of the elaborate molecular architecture in the C-terminal helical region of apoA-I to exert lipid efflux f