Speaker : Yoon Shin Park, Ph.D. (Research Professor, Ewha Womans University Medical School)
Date : 2012-08-07
Location : Room 106，Pharmacy Hall, Dankook University
Abstract : Cell permeable peptides (CPPs) are known for their versatility in carrying macro- or supramolecules through the cell membrane barriers that challenge the conventional drug-delivery approaches. The CPPs are capable of transporting their cargos, often linked by a covalent bond, into almost all cell types. Among such CPPs, we previously reported a new CPP, low molecular weight protamine (LMWP) peptide (VSRRRRRRGGRRRR) developed by enzymatic digestion of protamine (an FDA-approved drug), as a potent yet nontoxic CPP or membrane translocalization carrier. Both in vitro and animal investigations demonstrated that, via covalent or electrostatic conjugation, LMWP was able to transduce its attached protein, gene or carrier cargo into various types of cells. The LMWP offers distinct advantages. First, LMWP is as potent as the virus-derived TAT peptide, the most-studied CPP to date, in mediating cellular translocation of the attached cargos. Secondly, unlike other CPPs, the toxicity profile of LMWP has already been thoroughly established. LMWP was shown to be nonimmunogenic, and its use in dogs did not elicit acute toxic responses. Lastly, while other CPPs must be chemically synthesized, LMWP can be produced in mass quantities direct from native protamine with limited processing time and cost. More recently, it was shown that cell translocation mediated by LMWP does not cause any perturbation or damage to the cell membrane. Therefore, we suggest that LMWP can be used as a tool to aid intracellular delivery of drugs into target cells.