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A new family of cyclic cell-penetrating peptides (CPPs) is discovered and differs 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 of 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-fold more active than CPP12 under high serum protein concentrations, presumably because of less protein binding. CPP 17 enters the cell primarily by direct translocation at relatively low concentration (≥5 μM).
This article was published in the following journal.
Name: Chembiochem : a European journal of chemical biology
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