Publications by authors named "Mana Kotani"
Article Synopsis
- Researchers developed a peptide called A2-17, known for its ability to penetrate cell membranes, and studied its effectiveness using three structural variations.
- They found that the efficiency of cell penetration is linked to the peptide's hydrophobic moment, particularly noting that the isomer A2-17 L14R/R15L has the highest hydrophobic moment and penetrates deeper into membranes.
- The study demonstrated that while A2-17 L14R/R15L causes significant membrane damage, optimal perturbation of the membrane is essential for efficient cell entry without creating stable pores.
In the direct cell membrane penetration, arginine-rich cell-penetrating peptides are thought to penetrate into cells across the hydrophobic lipid membranes. To investigate the effect of the amphipathic property of arginine-rich peptide on the cell-penetrating ability, we designed a novel amphipathic cell-penetrating peptide, A2-17, and its derivative, A2-17KR, in which all lysine residues are substituted with arginine residues, based on the glycosaminoglycan binding region in the N-terminal α-helix bundle of human apolipoprotein E. Isothermal titration calorimetry showed that A2-17 variants have a strong ability to bind to heparin with high affinity.
View Article and Find Full Text PDF