Bunch berry
Docking
Human acetylcholinesterase (hAchE)
Human carbonic anhydrase II (hCA-II)
Human carboxylesterase I (hCES-I)
Lantana camara
Journal
Saudi journal of biological sciences
ISSN: 1319-562X
Titre abrégé: Saudi J Biol Sci
Pays: Saudi Arabia
ID NLM: 101543796
Informations de publication
Date de publication:
Dec 2023
Dec 2023
Historique:
received:
14
09
2023
revised:
11
10
2023
accepted:
19
10
2023
medline:
14
11
2023
pubmed:
14
11
2023
entrez:
14
11
2023
Statut:
ppublish
Résumé
Bunch berry ( In this study, we intended to assess twenty chosen constituents of Bunch berry as potent inhibitory agents of human acetylcholinesterase (hAchE), carbonic anhydrase II (hCA-II) and carboxylesterase 1 (hCES-1) employing in The twenty chosen Bunch berry components were examined about docking behaviour of hAchE, hCA-II and hCES-I by using the Swissdock method. Apart from to docking, Molecular physico-chemical, drug-likeness, ADME (ingesting, dispersing, metabolising, and excreting), and toxicity assessments were also performed utilising the Molinspiration, Swiss ADME, pkCSM, and STITCH web sites, correspondingly. Eight ligands (40 %) have exhibited strict adherence to Lipinski's rule of five (Ro5), according to molecular physico-chemical study. Drug-likeness property analysis has shown that five ligands (25 %) of Bunch berry predicted to exhibit moderate bioactivity score against all the descriptors. ADME analysis has shown that five ligands (25 %) of Bunch berry are predicted to possess high gastrointestinal absorption property Toxicity analysis has shown that six ligands (30 %) of Bunch berry are predicted to have hERG II (Human ether-a-go-go-related gene) inhibition activity. According to the docking analysis, lantic acid has the lowest atomic binding energy for all three target enzymes, hAchE (-6.23 kcal/mol), hCA-II (-4.46 kcal/mol), and hCES-I (-5.99 kcal/mol), respectively. Thus the current find provides an advanced understanding the twenty selected ligands of Bunch berry as potent inhibitory agents of human acetylcholinesterase (hAchE), carbonic anhydrase II (hCA-II) and carboxylesterase 1 (hCES-1).
Sections du résumé
Background
UNASSIGNED
Bunch berry (
Objective
UNASSIGNED
In this study, we intended to assess twenty chosen constituents of Bunch berry as potent inhibitory agents of human acetylcholinesterase (hAchE), carbonic anhydrase II (hCA-II) and carboxylesterase 1 (hCES-1) employing in
Methods
UNASSIGNED
The twenty chosen Bunch berry components were examined about docking behaviour of hAchE, hCA-II and hCES-I by using the Swissdock method. Apart from to docking, Molecular physico-chemical, drug-likeness, ADME (ingesting, dispersing, metabolising, and excreting), and toxicity assessments were also performed utilising the Molinspiration, Swiss ADME, pkCSM, and STITCH web sites, correspondingly.
Results
UNASSIGNED
Eight ligands (40 %) have exhibited strict adherence to Lipinski's rule of five (Ro5), according to molecular physico-chemical study. Drug-likeness property analysis has shown that five ligands (25 %) of Bunch berry predicted to exhibit moderate bioactivity score against all the descriptors. ADME analysis has shown that five ligands (25 %) of Bunch berry are predicted to possess high gastrointestinal absorption property Toxicity analysis has shown that six ligands (30 %) of Bunch berry are predicted to have hERG II (Human ether-a-go-go-related gene) inhibition activity. According to the docking analysis, lantic acid has the lowest atomic binding energy for all three target enzymes, hAchE (-6.23 kcal/mol), hCA-II (-4.46 kcal/mol), and hCES-I (-5.99 kcal/mol), respectively.
Conclusions
UNASSIGNED
Thus the current find provides an advanced understanding the twenty selected ligands of Bunch berry as potent inhibitory agents of human acetylcholinesterase (hAchE), carbonic anhydrase II (hCA-II) and carboxylesterase 1 (hCES-1).
Identifiants
pubmed: 37961045
doi: 10.1016/j.sjbs.2023.103847
pii: S1319-562X(23)00292-9
pmc: PMC10638019
doi:
Types de publication
Journal Article
Langues
eng
Pagination
103847Informations de copyright
© 2023 The Authors.
Déclaration de conflit d'intérêts
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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