| 초록 |
We developed a new type of cell penetrating peptides (CPPs) which contain multimeric a-helical leucine (L) and lysine (K)-rich seqeunces. Antiparallel LK dimeric peptides can effectively penetrate cells at 10 nM, a 1,000-fold lower concentration than the penetrable concentrations of conventional CPPs. Since the antiparallel conformation of the alpha helical peptides is similar to natural helix-loop-helix (HLH) motifs in proteins, we further developed multimeric HLH peptides, and generated fusion proteins containing different numbers of multimeric CPP motifs by the genetic engineering. Multimeric CPP-fused proteins can rapidly penetrate cells at much lower concentrations than monomeric or dimeric CPP-fused correspondents. As the first step of the biomedical application, we were able to induce adipocyte differentiation effectively by delivering the multimeric CPP-fused form of a transcription factor at nanomolar concentrations. |
