Nanobiological Studied on Drug Design using by Molecular Mechanic Method

سال انتشار: 1394
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 562

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شناسه ملی سند علمی:

CRSTCONF01_547

تاریخ نمایه سازی: 27 اسفند 1394

چکیده مقاله:

Influenza H1N1 is very important worldwide and point mutations that occur in virus Gene is a threat for World Health Organization (WHO) and druggists, which make this virus be resistant A (H1N1) virus to previous Antibiotic. Influenza epidemics cause severe respiratory illness in 30 million to 50 million people and kill 250 thousand to 500 thousand people worldwide every year. Today drug design is not in trial and error way , because of cost and wasting time, bioinformatics studies is essential for drug design . In this paper, we studied binding site Neuraminidase( NA) enzyme, (that is very important in drug design) in 310K temperatures and different dielectrics, for the best drug design. Information of NA enzyme was extracted from data bank protein (PDB) and NCBI sites. The new sequences of N1 were downloaded from NCBI influenza virus sequence database. Drug binding sites were assimilated and homology modeling using Argus lab 4.0, HyperChem 6.0 and Chem. D3 soft wares. Their stability was assessed in different dielectrics and temperatures.

کلیدواژه ها:

Neuraminidase enzyme – Influenza A (H1N1) – Binding site –Molecular Mechanic

نویسندگان

Maryam Mousavi

P.hD Student, Zanjan University of Medical Sciences,Zanjan, Iran& Department of pathology Amir – momenis Hospital

Seyed Reza Hosseini

Zanjan University of Medical Sciences,Zanjan,Iran

Davood Sohrabi

Assistant Professor, Department of Community Medicine, School of Medicine, Zanjan University of Medical Sciences, Zanjan, Iran

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