Catechin from Anonna senegalensis is a Potential Inhibitor of Erectile Dysfunction: Implication for Its Use in Male Sexual Enhancement

Erectile dysfunction (ED) is a major challenge for men. The drugs for its treatment are associated with side effects. Hence, in phytomedicinal research, where Anonna senegalensis ( A. senegalensis ) is a candidate with abundant phytochemicals possessing various pharmacological properties, but the se...

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Veröffentlicht in:Applied biochemistry and biotechnology 2023-08, Vol.195 (8), p.4936-4964
Hauptverfasser: Folawiyo, Moshood Abiola, Omotuyi, Idowu Olamiposi, Ajao, Folashade Omobolanle, Besong, Elizabeth, Adelusi, Temitope Isaac, Ajayi, Ayodeji Folorunsho
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Sprache:eng
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Zusammenfassung:Erectile dysfunction (ED) is a major challenge for men. The drugs for its treatment are associated with side effects. Hence, in phytomedicinal research, where Anonna senegalensis ( A. senegalensis ) is a candidate with abundant phytochemicals possessing various pharmacological properties, but the sex-enhancing phytochemical is elusive in the literature. This study aimed to understand the molecular interaction of its potent molecule mediating male sexual enhancement. A library of 69 compounds from A. senegalensis was docked against the ED-targeted proteins. Sildenafil citrate was used as the reference standard. Thereafter, the lead compound was screened for drug-likeness by applying the Lipinski rule of 5 (RO5), pharmacokinetic properties, and bioactivity using SwissADME and Molinspiration web servers, respectively. The results show catechin as the lead phytochemical compound with a stronger binding affinity for most of the proteins of ED. Also, catechin demonstrates good compliance with the RO5, great pharmacokinetic profiles, and could be said to be a polypharmacological molecule with good bioactivity scores. The research findings unravel the potential of catechin (a phytochemical belonging to the flavonoids class) from A. senegalensis leaf as a potential male sexual enhancement molecule via its high binding affinity for most erectile dysfunction-targeted proteins. They may require further toxicity and therapeutic evaluations in vivo.
ISSN:0273-2289
1559-0291
1559-0291
DOI:10.1007/s12010-023-04557-z