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Cyclic Cell‐Penetrating Peptides with Single Hydrophobic Groups
Author(s) -
Song Jian,
Qian Ziqing,
Sahni Ashweta,
Chen Kuangyu,
Pei Dehua
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.201900370
Subject(s) - chemistry , residue (chemistry) , side chain , cyclic peptide , alkyl , cell , arginine , peptide , biophysics , stereochemistry , biochemistry , chromosomal translocation , amino acid , organic chemistry , biology , gene , polymer
A new family of cyclic cell‐penetrating peptides (CPPs) has been discovered; they differ from previously reported cyclic CPPs by containing only a single hydrophobic residue. The optimal CPP structure consists of four arginine residues and a hydrophobic residue with a long alkyl chain (e.g., a decyl group) in a cyclohexapeptide ring. The most active member of this family, CPP 17 , has an intrinsic cellular entry efficiency similar to that of cyclic CPP12, the most active CPP reported to date. However, CPP 17 is 2.8 times more active than CPP12 under high serum protein concentrations, presumably because of the lower protein binding. CPP 17 enters the cell primarily by direct translocation at a relatively low concentration (≥5 μ m ).