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by any one of the type III enzymes. This can be achieved by the use of a 3′-phosphoramidite derivative of guanosine triphosphate (GTP). The incorporated guanosine moiety is essential for recognition of the glycogen phosphorylase by the protein domain involved in the recognition of the ribozyme. The guanosine moiety is replaced by diphosphate or phosphoramidite derivatives in the process of aminoacylation of the ribozyme. This way, the first and second specific RNA-binding regions in the ribozyme can be replaced by DNA oligonucleotides of appropriate sequence. The third specific RNA-binding region is preserved in the DNA oligonucleotide and is responsible for binding of the ribozyme to the ribosome.
The principal concern in designing such an antisense molecule is to find the sequence of DNA, which binds in the 3′-UTR of the target mRNA in the cell with high affinity. In order to be useful, it should not bind to other cellular RNAs with high affinity. In the case of ribozymes, the ribozyme must be inactive under conditions found in the cell. Thus, the choice of a ribozyme requires a thorough understanding of the biological context under which it will operate. The performance of an antisense oligonucleotide in a cell depends on its interaction with the RNAs in the cell. The binding sites for such an oligonucleotide must compete with the cellular RNAs for access to the target RNA. Because an oligonucleotide can bind to a number of cellular RNAs, it may not be possible to identify a specific target RNA that will be specifically bound by an oligonucleotide. Thus, for antisense therapies, chemical modification of the oligonucleotides may be required. For example, the 2′-position of pyrimidines can be modified to form 2′-5′-linked oligonucleotides, to increase resistance to degradation by endonucleases and to enhance the affinity for target RNA (Zamecnik and