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Collagen‐like Cell‐Penetrating Peptides
Author(s) -
Yamazaki Chisato M.,
Nakase Ikuhiko,
Endo Hiroyuki,
Kishimoto Saya,
Mashiyama Yoshihiro,
Masuda Ryo,
Futaki Shiroh,
Koide Takaki
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201301266
Subject(s) - heterotrimeric g protein , proteases , hydroxyproline , chemistry , triple helix , cell , peptide , biochemistry , computer science , computational biology , biology , stereochemistry , enzyme , receptor , g protein
Arginine‐rich heterotrimeric collagen‐like peptides were prepared, and their cellular uptake efficiency was evaluated. The spatial arrangement of the Arg residues (blue in picture) on the triple‐helix surface significantly affected the efficacy of the cellular uptake. The collagen‐like triple‐helical conformation provides these cell‐penetrating peptides with a high resistance to proteases. O= L ‐4‐hydroxyproline.