Loosening of Lipid Packing by Cell‐Surface Recruitment of Amphiphilic Peptides by Coiled‐Coil Tethering. (9th August 2019)

• Record Type: Journal Article
• Authors: Sakai, Takayuki; Kawano, Kenichi; Iino, Masatomo; Takeuchi, Toshihide; Imanishi, Miki; Futaki, Shiroh
• Is Part Of: Chembiochem. Volume 20:Number 16(2019)
• Page Start: 2151
• Page End: 2159
• Publication Date: 2019-08-09
• Subjects: amphiphiles -- helical structures -- lipid packing -- membranes -- peptides; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201900347
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: 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. Abstract : Bound to bend : An amphiphilic helical peptide derived from the N‐terminal segment of epsin‐1 (EpN18), with the ability to induce curvature and loosen lipid packing, has been effectively recruited to cell surfaces in a reversible manner through coiled‐coil tethering to protein expressed on the cell surface.