Effect of amino acid distribution of amphipathic helical peptide derived from human apolipoprotein A-I on membrane curvature sensing.
Amphipathic helix, which senses membrane curvature, is of growing interest. Here we explore the effect of amino acid distribution of amphipathic helical peptide derived from the C-terminal region (residues 220-241) of human apolipoprotein (apo) A-I on membrane curvature sensing. This peptide preferred a curved membrane in a manner similar to full-length apoA-I, although its model peptide did not sense membrane curvature. Substitution of several residues both on the polar and non-polar 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 function.
Department of Biophysical Chemistry, Kobe Pharmaceutical University, Higashinada-ku, Kobe, Japan. masatnk@kobepharma-u.ac.jp
Masafumi
M
Tanaka
Yuki
Y
Takamura
Toru
T
Kawakami
Saburo
S
Aimoto
Hiroyuki
H
Saito
Takahiro
T
Mukai
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D016632:Apolipoprotein A-I / Q000737:chemistry* / Q000235:genetics; D002942:Circular Dichroism; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008567:Membranes, Artificial; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics; D010743:Phospholipids / Q000737:chemistry; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013816:Thermodynamics; D053835:Unilamellar Liposomes / Q000737:chemistry
D016632:Apolipoprotein A-I; D008567:Membranes, Artificial; D010446:Peptide Fragments; D010743:Phospholipids; D053835:Unilamellar Liposomes