Seyed hashem Daryabari, - Chemical Injuries Research Center, Systems biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran,Iran
Hossein Aghamollaei, - Chemical Injuries Research Center, Systems biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran,Iran
Mahdi Naderi, - Chemical Injuries Research Center, Systems biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran,Iran
Khosrow Jadidi - Chemical Injuries Research Center, Systems biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran,Iran

Purpose: . The aim of this study was to in-silico evaluation of 8-amino acids peptides for inhibition of crystallin proteins aggregation. Methods: Firstly, the model of 3D structure of human mutated crystallins was designed using bioinformatics tools. Then , three different 8- amino acids peptide were evaluated for their potency for inhibition of protein oligomerization and crystalline aggregation. The binding site of these peptides to the crystallins was determined. Results: Bioinformatics variables showed that the 3D model of crystallins are reliable. Designed peptides can bind to mutated Gamma crystalline efficiently. The results showed that peptides affinity to gamma crystalline inhibited protein-protein interaction and reduced oligomerization and aggregation of gamma crystallins. The binding site of these peptides on the crystallin are different.Conclusion: In silico analysis approved that these peptides can prevent aggregation of crystalline proteins. After more confirmation in experimental studies, these peptides can be introduced as new candidates for treatment of congenital cataract.