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Nucleic Acids Symposium Series 2009 53(1):55-56; doi:10.1093/nass/nrp028
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© 2009 Oxford University Press

This article appears in the following Nucleic Acid Symposium Series issue: The 6th International Symposium on Nucleic Acids Chemistry (36th Symposium on Nucleic Acids Chemistry) [View the issue table of contents]

Studies on the effects of arginine residues introduced to peptide ribonucleic acids (PRNA) on the complex stability with RNA

Akihiro Nishio2, Nobuya Sawa2, Keiko Onodera1, Seiji Sakamoto1, Yasuyuki Araki1, Ikuhiko Nakase3, Shiroh Futaki3, Yoshihisa Inoue2 and Takehiko Wada1,*

1Institute of Multidisciplinary Research for Advanced Materials (IMRAM), Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai 980-8577, Japan, 2Department of Applid Chemistry, Graduate School of Engineering, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan and 3Institute for Chemical Reseach, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan

*Corresponding author. E-mail: hiko{at}tagen.tohoku.ac.jp

Abstract

In this study, a series of novel {alpha}-Peptide ribonucleic acid ({alpha}-PRNA) oligomers, possessing alternative {alpha}-PRNA/arginine or serine sequences, were newly designed, synthesized, and evaluated as the third-generation PRNA. As expected, these {alpha}-PRNAs formed highly stable sequence-specific complexes with the complementary RNAs, for which both the conventional hydrogen-bonding interactions between the complementary nucleobase pairs and the electrostatic interactions between the arginine's guanidinium cation and the RNA's phosphate anion on the backbone are jointly responsible. Moreover, in the cases of {alpha}-PRNA and single point mismatched DNA mixing systems, appreciable Tm could not be observed, thus {alpha}-PRNAs containing Arg were expected to have high nucleobase sequence discrimination abilities. It was demonstrated that the recognition behavior of {alpha}-PRNA with Arg/Ser backbone with complementary RNA can be controlled externally through the orientation change of pyrimidine nucleobase induced by borate ester formation of the ribose's 2',3'-cis-diol.


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