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concentration. We at first checked by HPLC and MS whether calpain I could digest theLmyc smoothly. Then digestion experiments using the DNA-PNA quadruplex wereconducted. It was found that Tm of the DNA with digested peptides by calpain I wasalmost equal to that of DNA alone. This implied that quadruplex structure of halfTG andLmyc is destabilized by calpain I.With more improvement of binding-specificity and adding other functions such ascellular penetrating, this system may lead to controls of the DNA and/or RNA eventsincluding RNA expression. Throughout this study, these PNA-peptide conjugates would beone of the promising tools for regulation of important cellular events toward cellengineering and tissue engineering.Fig. 2. Outline drawing of the switching system for regulation of G-quadruplex structureusing Lmyc.AcknowledgmentsThis study was in part supported by the Grants-in-Aid for Scientific Research, the "Core research"project (2009-2014) from the Ministry of Education, Culture, Sports, Science and Technology(MEXT). K. U. is grateful to Grant-in-Aid for Research Activity Start-up from MEXT.References1. Miyoshi, D., Matsumura, S., Nakano, S., Sugimoto, N. J. Am. Chem. Soc. 126, 165-169 (2003).2. Yu, H.Q., Miyoshi, D., Sugimoto, N. J. Am. Chem. Soc. 128, 15461-15468 (2006).3. Yaku, H., Murashima, T., Miyoshi, D., Sugimoto, N. Chem. Commun. 46, 5740-5742 (2010).4. Sano, S., Tomizaki, K.-Y., Usui, K., Mihara, H. Bioorg. Med. Chem. Lett. 16, 503-506 (2006).5. Roy, S., Tanious, F.A., Wilson, W.D. Ly, D.H. Armitage, B.A. Biochemistry 46, 10433-10443(2007).609