Claim · model-written summary
Isorhamnetin docked to myeloperoxidase with a binding affinity of -9,4 kcal/mol.
- Taxon
- H.scabrum and H. triquetrifolium
Hypericum triquetrifolium
Hypericum scabrume1 - Outcome
- binding affinitye0
- Value
- -9,4 kcal/mole0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.


Verbatim
e0“With a binding affinity of -9,4 kcal/mol, the isorhamnetin docks to the active site of the myeloperoxidase enzyme.”
e1“H.scabrum and H. triquetrifolium species”
Title
Turgut Taşkın; Mizgin Ermanoğlu; Erkan Rayaman; et al. Brazilian Archives of Biology and Technology 2024. doi:10.1590/1678-4324-2024240063
Other claims from this paper (7)
- Observation Methanol extracts of the two Hypericum species had high total phenolic content.
- Observation The extracts showed potent anti-urease, anti-crystallization and antimicrobial activity.
- Observation Methanol extracts showed no toxicity in the L-929 cell line.
- Observation The methanol extracts contained quantified isorhamnetin, rutin and chlorogenic acid.
- Observation Chlorogenic acid docked to xanthine oxidase with a binding affinity of -10.3 kcal/mol.
- Observation Rutin docked to myeloperoxidase with a binding affinity of -9,9 kcal/mol.
- Observation The phenolic compounds were predicted to lack mutagenic and hepatotoxic effects.