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Molecular Biology Research Communications، جلد ۳، شماره ۲، صفحات ۱۱۵-۱۲۷
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عنوان انگلیسی Designing and analyzing the structure of Tat-BoNT/A(1-448) fusion protein: An in silico approach
چکیده انگلیسی مقاله Clostridium botulinum type A (BoNT/A) produces a neurotoxin recently found to be useful as an injectable drug for the treatment of abnormal muscle contractions. The catalytic domain of this toxin which is responsible for the main toxin activity is a zinc metalloprotease that inhibits the release of neurotransmitter mediators in neuromuscular junctions. A cell penetrating cationic peptide, Tat, which is a truncated N-terminal part of the Tat protein from human immunodeficiency virus, can help the toxin penetrate the skin uninvasively. This study aimed at an in silico analyses of the Tat-BoNT/A(1-448) fusion protein structure. A genomic construct was designed and optimized based on E. coli codon usage. The structure of mRNA as well as the properties of hypothetical chimeric protein was then analyzed by bioinformatic tools. Afterwards, the secondary and tertiary structures of the fusion protein were predicted by GOR4 and I-TASSER online web servers. The interaction with synaptosomal associated protein 25kDa (SNAP-25) was also analyzed as a natural substrate for the toxin. Based on the studied secondary and tertiary structures of the protein, the selected order of fusion proteins provides the natural activity of each peptide. Energy calculating data show that the acquired thermodynamic ensemble related to the mRNA structure was-1473.2 kJ/mol (-352.10 kcal/mol) and both total protein energy (Etotal) and shape related energy (Eshape) were calculated as -2294.2kJ/mol (-548.32 kcal/mol). The stability index of TAT-BoNT/A was computed to be 27.22 which has an acceptable stability as compared to that of native BoNT/A (22.39). 
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نویسندگان مقاله جعفر امانی |
applied microbiology research center, baqiyatallah university of medical sciences, tehran, iran.
سازمان اصلی تایید شده: دانشگاه علوم پزشکی بقیه الله (Baqiyatallah university of medical sciences)

پروانه صفاریان |
department of bacteriology, faculty of medical sciences, tarbiat modares university, tehran, iran.
سازمان اصلی تایید شده: دانشگاه تربیت مدرس (Tarbiat modares university)

شاهین نجار پیرایه | najar pirayeh
department of bacteriology, faculty of medical sciences, tarbiat modares university, tehran, iran
سازمان اصلی تایید شده: دانشگاه تربیت مدرس (Tarbiat modares university)

عباسعلی ایمانی فولادی | abbas ali imani fooladi
applied microbiology research center, baqiyatallah university of medical sciences, tehran, iran.
سازمان اصلی تایید شده: دانشگاه علوم پزشکی بقیه الله (Baqiyatallah university of medical sciences)

نشانی اینترنتی http://mbrc.shirazu.ac.ir/article_2038_4bd6673b01f2fb3a48ef1155ae3fbdd2.pdf
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