Asma Soofi - Department of Physical Chemistry, School of Chemistry, University College of Science
Hassan Behnejad - Department of Physical Chemistry, School of Chemistry, University College of Science
Jahan B Ghasemi - Department of Analytical Chemistry, School of Chemistry, University College of Science, University of Tehran, Tehran ۱۴۱۵۵, Iran ۱۶th Azar St., Enghelab Sq., Tehran, Iran

In continue with our recent studies on the claudins as a class of blood-brain barrier (BBB)and very good target for the specific channel of the drug delivery systems, in this part we aregoing to focus on the dynamic behavior and thermodynamic stability of the of claudin embeddedin DMPC membrane, in 3 different temperature by RMSD. About twenty different claudins arerecognized until now which are classified into two part, classical and nonclassified protein. Bydetailed researches on (BBB), it has been reported that (BBB) is constructed mostly by claudin-5which is an integral protein. It has been driven from recent studies that accuracy of homologymodel with the atomistic MD simulations, showed how the hydrophobic residues providestructural stability to the monomeric structure and effect on drug transport from blood to brainMD simulations were performed using GROMACS. The lowest energy model of the protein wasembedded in a DMPC bilayer for simulation with explicit TIP3 water model three differenttemperature and 0.15 M, KCl solution. The simulations used the CHARMM36 force fieldparameters for proteins, lipid, and water. As an acknowledgment to previous studies flexibleregions e.g. Large loops unwound termini can cause large contributions to RMSD and foranother stabilitiy Cα RMSF which is a measure of the local chain flexibility shows morefluctuations for residues which are in direct contact with solutions as an example (r:30-47).

Blood, Brain Barrier, GROMACS, RMSD