期刊
CHEMICAL PHYSICS
卷 419, 期 -, 页码 78-83出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.chemphys.2012.12.041
关键词
Phospholipid; Flip-flop; Transmembrane peptide; Small-angle neutron scattering; Fluorescence; Dithionite assay
资金
- Japanese Ministry of Education, Culture, Sports, Science and Technology [22018015, 23107718]
- Inamori Foundation
- Grants-in-Aid for Scientific Research [22018015, 25610120] Funding Source: KAKEN
We designed three types of transmembrane model peptides whose sequence originates from a frequently used model peptide KALP23, and we investigated their effects on phospholipid flip-flop. Time-resolved small-angle neutron scattering and a dithionite fluorescent quenching assay demonstrated that TMP-L, which has a fully hydrophobic transmembrane region, did not enhance phospholipid flip-flop, whereas TMP-K and TMP-E, which have Lys and Glu, respectively, in the center of their transmembrane regions, enhanced phospholipid flip-flop. Introduction of polar residues in the membrane-spanning helices is considered to produce a locally polar region and enable the lipid head group to interact with the polar side-chain inside the bilayers, thereby reducing the activation energy for the flip-flop. A bioinformatics approach revealed that acidic and basic residues account for 4.5% of the central region of the transmembrane domain in human ER membrane proteins. Therefore, polar residues in ER membrane proteins are considered to provide flippase-like activity. (C) 2013 Elsevier B.V. All rights reserved.
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