Analysis of Docking Study on Protein Neprilysin (Neutral Endopeptidase) Inhibition for Anti-aging Treatment by Aloe Emodin and Aloe Emodin Carbonyl Derivative

Abstract

Attempts were made to perform comparative docking study of Aloe emodin and its derivative on Neprilysin (PDB code: 1R1J) by using VLife MDS software to ascertain the activity of both.  From all the interactions (Hydrogen bond and vander waals) it was observed that, the common amino acids which interacts with the common ligand were ASN542A, ALA543A, ARG102A, ASN542A, VAL580A. The result showed that the AEC
(–1790.15 KCal) showed high total binding energy (ΔG) as compared to AE (–1289.55 KCal). Interactions of AEC reference ligand with protein NEP were studied. The results revels high vander wall bond interaction compared to hydrogen bond among different amino acid. The compound may be the most active anti-aging agent as per Docking results. The compound AEC was most active while compound AE was least active as per docking.

Keywords: Docking, antiaging, Aloe emodin, Neprilysin