Open AccessScreening of druggable conformers of α-synuclein using molecular dynamics simulation
Author(s) -
Dorothy Das,
Mridusmita Kakati,
Aroon Gracy,
Airy Sanjeev,
Swarna M. Patra,
Venkata Satish,
Kumar Mattaparthi
Publication year - 2020
Publication title -
biointerface research in applied chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.216
H-Index - 11
ISSN - 2069-5837
DOI - 10.33263/briac103.338347
Subject(s) - druggability , conformational isomerism , radius of gyration , molecular dynamics , sasa , intrinsically disordered proteins , small molecule , accessible surface area , chemistry , crystallography , molecule , computational chemistry , biology , biochemistry , organic chemistry , paleontology , gene , polymer
Intrinsically disordered proteins (IDPs) are becoming an engaging prospect for therapeutic intervention by small drug-like molecules. IDPs structural binding pockets and their flexibility exist as a challenging target for standard druggable approaches. Hence, in this study, we have performed and identified the most probable druggable conformers from molecular dynamics simulation on α-synuclein based on the structural parameters: radius of gyration (Rg), solvent accessible surface area (SASA) and the standard secondary structure content. We found the conformers showing lower solvent accessible surface area and higher secondary structure content of α-helical are defined to be suitable binding pockets for druggability.