Membrane anchoring of a curvature-inducing peptide, EpN18, promotes membrane translocation of octaarginine
K Kuroki, T Sakai, T Masuda, K Kawano… - Bioorganic & Medicinal …, 2021 - Elsevier
K Kuroki, T Sakai, T Masuda, K Kawano, S Futaki
Bioorganic & Medicinal Chemistry Letters, 2021•ElsevierEpN18 is a curvature-inducing peptide, which loosens lipid packing upon interaction with
the cell membrane, and facilitates cell-membrane penetration by arginine-rich cell-
penetrating peptides, including octaarginine (R8). In the present study, we conjugated the N-
terminal of EpN18 with a pyrenebutyryl (pBu) moiety, which acts as an anchoring unit that
increases membrane interactions. Enhanced lipid-packing loosening and cytosolic
translocation of R8 were observed by the pBu anchoring of EpN18.
the cell membrane, and facilitates cell-membrane penetration by arginine-rich cell-
penetrating peptides, including octaarginine (R8). In the present study, we conjugated the N-
terminal of EpN18 with a pyrenebutyryl (pBu) moiety, which acts as an anchoring unit that
increases membrane interactions. Enhanced lipid-packing loosening and cytosolic
translocation of R8 were observed by the pBu anchoring of EpN18.
Abstract
EpN18 is a curvature-inducing peptide, which loosens lipid packing upon interaction with the cell membrane, and facilitates cell-membrane penetration by arginine-rich cell-penetrating peptides, including octaarginine (R8). In the present study, we conjugated the N-terminal of EpN18 with a pyrenebutyryl (pBu) moiety, which acts as an anchoring unit that increases membrane interactions. Enhanced lipid-packing loosening and cytosolic translocation of R8 were observed by the pBu anchoring of EpN18.
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