دوره 5، شماره 2 - ( 2-1396 )                   جلد 5 شماره 2 صفحات 33-28 | برگشت به فهرست نسخه ها


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Ahmadi N A, Esmaeili A, Javadi Zarnaghi F. Bioinformatics Designing of 10-23 Deoxyribozyme against Coding Region of Beta-galactosidase Gene . Res Mol Med (RMM) 2017; 5 (2) :28-33
URL: http://rmm.mazums.ac.ir/article-1-240-fa.html
Bioinformatics Designing of 10-23 Deoxyribozyme against Coding Region of Beta-galactosidase Gene . Research in Molecular Medicine. 1396; 5 (2) :28-33

URL: http://rmm.mazums.ac.ir/article-1-240-fa.html


چکیده:   (12225 مشاهده)
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.
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نوع مطالعه: پژوهشي | موضوع مقاله: آمار زیستی
انتشار: 1396/6/14

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