Non-Covalent Binding of Disodium Disuccinate Astaxanthin to the Catalytic Site of Phosphodiesterase 5A: A Molecular Modeling Study

Title: Non-Covalent Binding of Disodium Disuccinate Astaxanthin to the Catalytic Site of Phosphodiesterase 5A: A Molecular Modeling Study

Volume: 4 Issue: 2

Author(s): Eszter Hazai, Zsolt Bikadi, Ferenc Zsila and Samuel F. Lockwood

Affiliation:

Keywords: Astaxanthin, Cardax, Carotenoids, Disodium disuccinate astaxanthin, Docking, Phosphodiesterase 5A

Abstract: Phosphodiesterases are clinical targets for congestive heart failure, erectile dysfunction and inflammation. Intake of carotenoids decreases the risk of cardiovascular and inflammatory diseases. Therefore, phosphodiesterase binding of the carotenoid derivative disodium disuccinate astaxanthin (Cardax) was investigated using molecular modeling methods. Cardax was predicted to bind to PDE5A at the catalytic site.

Cite this article as:

Hazai Eszter, Bikadi Zsolt, Zsila Ferenc and Lockwood F. Samuel, Non-Covalent Binding of Disodium Disuccinate Astaxanthin to the Catalytic Site of Phosphodiesterase 5A: A Molecular Modeling Study, Letters in Drug Design & Discovery 2007; 4(2) . https://dx.doi.org/10.2174/157018007779422497