The discovery of Hsp70 domain with cell-penetrating activity.

摘要: Chaperone Hsp70 can cross the plasma membrane of living cells using mechanisms that so far have not received much research attention. Searching part molecule is responsible for transport ability Hsp70, we found a cationic sequence composed 20 amino acid residues on its surface, KST peptide, which was used in further experiments. We showed peptide enters various origins with same efficiency as full-length chaperone. capable carrying cargo molecular weight 30 times greater than own into cells. When compared membrane-crossing activity complex Avidin (KST–Av complex) similarly linked canonical TAT penetrated SK-N-SH human neuroblastoma at similar rate and peptide. Furthermore, carry protein complexes consisting specific antibody coupled to through bridge. An delivered high expression level reduced protective power chaperone sensitized pro-apoptotic effect staurosporine. studied penetration KST–Av inside erythroleukemia K-562 both an active intracellular mechanism included vesicular structures negatively charged lipid domains. Competition analysis conversely prevented dose-dependent manner. Electronic supplementary material The online version this article (doi:10.1007/s12192-014-0554-z) contains material, available authorized users.