Department of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio, 43210, USA.
School of Pharmacy, Guangdong Pharmaceutical University, Guangzhou, Guangdong Province, 510006, China.
Chembiochem. 2019 Aug 16;20(16):2085-2088. doi: 10.1002/cbic.201900370. Epub 2019 Jul 24.
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 μm).
现已发现一类新型的环状细胞穿透肽（CPP）；与之前报道的环状 CPP 不同，它们仅含有一个疏水性残基。最佳 CPP 结构由四个精氨酸残基和一个疏水性残基组成，该残基带有长烷基链（例如癸基），形成环己六肽环。该家族中最活跃的成员 CPP17 的细胞内进入效率与目前报道的最活跃的 CPP12 相似。然而，在高血清蛋白浓度下，CPP17 的活性比 CPP12 高 2.8 倍，这可能是因为 CPP17 的蛋白结合率较低。CPP17 主要通过直接转位在相对较低的浓度（≥5μm）进入细胞。
