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Loosening of Lipid Packing by Cell‐Surface Recruitment of Amphiphilic Peptides by Coiled‐Coil Tethering
Author(s) -
Sakai Takayuki,
Kawano Kenichi,
Iino Masatomo,
Takeuchi Toshihide,
Imanishi Miki,
Futaki Shiroh
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900347
Subject(s) - leucine zipper , membrane , biophysics , chemistry , amphiphile , zipper , cell membrane , cell , peptide , biochemistry , peptide sequence , biology , organic chemistry , polymer , algorithm , copolymer , gene , computer science
Lipid packing has a strong influence on the formation and structural dynamics of cell membranes. Techniques to modulate lipid packing may thus enable modification of cellular functions and events. An 18‐residue amphiphilic helical peptide derived from the N‐terminal segment of epsin‐1 (EpN18) is reported to induce positive membrane curvature and to loosen lipid packing in the cell membrane. In this study, it is shown that EpN18, crosslinked to a leucine‐zipper peptide K4, is recruited to the cell surface by interacting with a cell‐surface‐expressed E3 leucine‐zipper segment. Cell‐surface tethering markedly enhanced loosening of lipid packing, which led to the promotion of membrane translocation of octaarginine. The loosening of lipid packing by EpN18 was also confirmed by analyzing the generalized polarization value with a membrane‐environment‐sensitive dye, 2‐hydroxy‐3‐{2‐[(2‐hydroxyethyl)dimethylamino]ethyl}‐4‐{2‐[6‐(dibutylamino)‐2‐naphthyl]ethenyl}pyridiniumdibromide (di‐4‐ANEPPDHQ). This approach thus shows promise for the control of lipid packing and related cellular events.