Non-covalent binding of disodium disuccinate astaxanthin to the catalytic site of phosphodiesterase 5A: A molecular modeling study

Eszter Hazai, Zsolt Bikádi, Ferenc Zsila, Samuel F. Lockwood

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)128-136
Number of pages9
JournalLetters in Drug Design and Discovery
Volume4
Issue number2
DOIs
Publication statusPublished - Mar 1 2007

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Keywords

  • Astaxanthin
  • Cardax
  • Carotenoids
  • Disodium disuccinate astaxanthin
  • Docking
  • Phosphodiesterase 5A

ASJC Scopus subject areas

  • Molecular Medicine
  • Pharmaceutical Science
  • Drug Discovery

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