Oleanolic acid purified from the stem bark of Olax subscorpioidea Oliv. inhibits the function and catalysis of human 17β-hydroxysteroid dehydrogenase 1

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F25%3A00641551" target="_blank" >RIV/61389030:_____/25:00641551 - isvavai.cz</a>

Alternative codes found

RIV/61989592:15310/24:73627874

Result on the web

<a href="https://doi.org/10.1080/07391102.2024.2423173" target="_blank" >https://doi.org/10.1080/07391102.2024.2423173</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1080/07391102.2024.2423173" target="_blank" >10.1080/07391102.2024.2423173</a>

Result language

angličtina

Original language name

Oleanolic acid purified from the stem bark of Olax subscorpioidea Oliv. inhibits the function and catalysis of human 17β-hydroxysteroid dehydrogenase 1

Original language description

Cancer is a leading cause of global death. Medicinal plants have gained increasing attention in cancer drug discovery. In this study, the stem bark extract of Olax subscorpioidea, which is used in ethnomedicine to treat cancer, was subjected to phytochemical investigation leading to the isolation of oleanolic acid (OA). The structure was elucidated by 1-dimensional and 2-dimensional nuclear magnetic resonance spectroscopic (NMR) data, and by comparing its data with previously reported data. Molecular docking was used to investigate the interactions of OA with nine selected cancer-related protein targets. OA docked well with human 17 beta-hydroxysteroid dehydrogenase type-1 (17 beta HSD1), caspase-3, and epidermal growth factor receptor tyrosine kinase (binding affinities:9.8,9.3, and9.1 kcal/mol, respectively). OA is a triterpenoid compound with structural similarity to steroids. This similarity with the substrates of 17 beta HSD1 gives the inhibitor candidate an excellent opportunity to bind to 17 beta HSD1. The structural and functional dynamics of OA-17 beta HSD1 were investigated by molecular dynamics simulations at 240 ns. Molecular mechanics/Poisson-Boltzmann surface area (MMPBSA) studies showed that OA had a binding free energy that is comparable with that of vincristine (-52.76, and63.56 kcal/mol, respectively). The average C-alpha root mean square of deviation (RMSD) value of OA (1.69 & Aring) compared with the unbound protein (2.01 & Aring) indicated its high stability at the protein's active site. The binding energy and stability at the active site of 17 beta HSD1 recorded in this study indicate that OA exhibited profound inhibitory potential. OA could be a good scaffold for developing new anti-breast cancer drugs.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

30107 - Medicinal chemistry

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2025

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Biomolecular Structure & Dynamics

ISSN

0739-1102

e-ISSN

1538-0254

Volume of the periodical

43

Issue of the periodical within the volume

14

Country of publishing house

GB - UNITED KINGDOM

Number of pages

14

Pages from-to

7949-7962

UT code for WoS article

001347002200001

EID of the result in the Scopus database

2-s2.0-85209072213