Docking studies of Tau Protein

Alzheimer’s disease (AD)[1] is a fatal brain disorder and alone in United States approximately 4.5 millions Americans are suffering from this disease which is expected by 2050 to range between 11.3 million to 16 million[2] Alzheimer’s disease is a form of dementia, in which nerve cells in memory areas of brain and eventually other areas begin to die at accelerated rate resulting in serious deterioration in several mental functions, such as loss in memory, language, orientation and judgment [3] AD is characterized by the formation of senile plaques (made of β amyloid, a toxic protein that comes from normal protein) and neurofibrillary tangles (followed by changes in tau protein) resulting in neuronal destructions. Currently available drugs against AD target the acetylcholine cycle thus stopping the abnormal breakdown of acetylcholine. The modern docking programs/software packages e.g. MOE, AcSite, Spdbv, and Rastop etc can be used to find the active site of the tau protein [4]. The ligand against this active binding site can be found by MOE. The exact confirmation and configuration of the ligand can be calculated to find the best molecule with minimum binding energy [5] and it can be used to develop potential drug molecules against the disease. This work is an attempt to find out the amino acid sequences responsible for biologically active structure which should enable us to design a lead molecule against the disease. In this work we have carried out the docking analysis of Tau protein responsible for AD. 50 structures after the docking were saved in the form of a database. The best five structures in terms of energy were taken, and the amino acids residues of the ligand and receptor molecule which bind to give the best biologically active conformation, were analyzed.