%0 Journal Article %A Ahmadi, Nasrin al-Sadat %A Esmaeili, Abolghasem %A Javadi Zarnaghi, Fatemeh %T Bioinformatics Designing of 10-23 Deoxyribozyme against Coding Region of Beta-galactosidase Gene %J Research in Molecular Medicine %V 5 %N 2 %U http://rmm.mazums.ac.ir/article-1-240-en.html %R 10.29252/rmm.5.2.28 %D 2017 %K 10-23 deoxyribozyme, gene expression, beta-galactosidase gene, %X Background: Deoxyribozymes (Dzs) can play a role as gene expression inhibitors at mRNA level. Among Dzs, the 10-23 deoxyribozyme has significant potentials for treatment of diseases. Designed Dz includes a catalytic core made of 15 deoxyribonucleotides and two binding arms consisted of 6-12 nucleotides for site specific binding to target RNA and hydrolysis. The enzyme has characteristic features for cleavage of the RNA target between an unpaired purine (A, G) and a paired pyrimidine (C or U). In this study, 10-23 Dz is designed for the coding region of the α-peptide of a lacZ gene. Material and Methods: The primary sequence of a plasmid with α-complementation ability was taken from addgene database. To confirm sequence validity, ExPASy was used to analyze related ORFs for the retrieved sequence. The ORF with identical sequence to α-peptide was selected in the reverse complement sequence. Subsequently, the secondary structure of the α-peptide was analyzed in DINAMelt web server and Mfold software. Then the intended target site was selected inside the coding region of the α-peptide. The Dzs sequence was designed for the target site with nucleotide binding arms. Results and conclusion: The resulted Dz in this study can be used as a promising catalytic DNA inside bacterial cells for blue-white screening. Criteria such as biological stability and catalytic rate of such enzymes must be evaluated in vivo and in vitro. %> http://rmm.mazums.ac.ir/article-1-240-en.pdf %P 28-33 %& 28 %! Designing of deoxyribozyme against lacZ %9 Research %L A-10-751-2 %+ Cellular and Molecular Biology Division; Department of Biology; Faculty of Sciences, University of Isfahan; Isfahan; Iran %G eng %@ 2322-1348 %[ 2017