title: Nanobiological studies on drug design using molecular mechanic method.
abstract: BACKGROUND
  Influenza H1N1 is very important worldwide and point mutations that occur in the virus gene are a threat for the World Health Organization (WHO) and druggists, since they could make this virus resistant to the existing antibiotics. Influenza epidemics cause severe respiratory illness in 30 to 50 million people and kill 250,000 to 500,000 people worldwide every year. Nowadays, drug design is not done through trial and error because of its cost and waste of time; therefore bioinformatics studies is essential for designing drugs.
  
  
  METHODS
  This paper, infolds a study on binding site of Neuraminidase (NA) enzyme, (that is very important in drug design) in 310K temperature and different dielectrics, for the best drug design. Information of NA enzyme was extracted from Protein Data Bank (PDB) and National Center for Biotechnology Information (NCBI) websites. The new sequences of N1 were downloaded from the NCBI influenza virus sequence database. Drug binding sites were assimilated and homologized modeling using Argus lab 4.0, HyperChem 6.0 and Chem. D3 softwares. Their stability was assessed in different dielectrics and temperatures.
  
  
  RESULTS
  Measurements of potential energy (Kcal/mol) of binding sites of NA in different dielectrics and 310K temperature revealed that at time step size = 0 pSec drug binding sites have maximum energy level and at time step size = 100 pSec have maximum stability and minimum energy.
  
  
  CONCLUSIONS
  Drug binding sites are more dependent on dielectric constants rather than on temperature and the optimum dielectric constant is 39/78.
authors.affiliation: Young Researchers and Elites Club, Science and Research Branch, Islamic Azad University, Tehran, Iran.
authors.forename: Hooria Seyedhosseini
authors.initials: HS
authors.lastname: Ghaheh
authors.affiliation: Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran.
authors.forename: Maryam
authors.initials: M
authors.lastname: Mousavi
authors.affiliation: Department of Pathology, Amir-Momenin Hospital, Isfahan University of Medical Sciences, Isfahan, Iran.
authors.forename: Mahmood
authors.initials: M
authors.lastname: Araghi
authors.affiliation: Young Researchers and Elites Club, Science and Research Branch, Islamic Azad University, Tehran, Iran.
authors.forename: Reza
authors.initials: R
authors.lastname: Rasoolzadeh
authors.affiliation: Department of Public Health, Isfahan University of Medical Sciences, Isfahan, Iran.
authors.forename: Zahra
authors.initials: Z
authors.lastname: Hosseini
keywords: Binding site; influenza A (H1N1); molecular mechanic; neuraminidase enzyme