In silico design of new inhibitors for crystalline aggregation as a new approach in treatment of congenital cataract

Session Details

Session Title: Posterior Capsule Opacification/IOL Power Calculations

Session Date/Time: Tuesday 17/09/2019 | 14:00-16:00

Paper Time: 15:02

Venue: Free Paper Forum: Podium 2

First Author: : S.Daryabari IRAN

Co Author(s): :    H. Aghamollaei   K. Jadidi   M. Naderi                       

Abstract Details

Purpose:

Congenital cataract is the primary cause of treatable childhood blindness worldwide. The crystallins have been demonstrated to be involved in cataractogenesis in human. Several mutations in α and β crystallin proteins were reported. These mutations led to protein- protein interaction, protein aggregation, denaturation and finally promotion of cataract. The aim of this study was to in-silico evaluation of 8-amino acids peptides for inhibition of crystallin proteins aggregation.

Setting:

Baqiyatallah university of medical sciences

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.

Conclusions:

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.

Financial Disclosure:

None