{rfName}
Me

Indexed in

Citations

59

Altmetrics

Analysis of institutional authors

Lamsabhi, Al MokhtarAuthor

Share

August 11, 2024
Publications
>
Article
No

Mechanistic insights into the metabolic pathways of vanillin: unraveling cytochrome P450 interaction mechanisms and implications for food safety

Publicated to: Organic & Biomolecular Chemistry. 22 (32): 6561-6574 - 2024-08-14 22(32), DOI: 10.1039/d4ob00973h

Authors:

Kamel, EM; Maodaa, S; Al-Shaebi, EM; Lamsabhi, A
[+]

Affiliations

Beni Suef Univ, Fac Sci, Chem Dept, Bani Suwayf 62514, Egypt - Author
King Saud Univ, Coll Sci, Dept Zool, POB 2455, Riyadh 11451, Saudi Arabia - Author
Univ Autonoma Madrid, Dept Quim, Campus Excelencia UAM CSIC Cantoblanco, Modulo 13, Madrid 28049, Spain - Author
Univ Autonoma Madrid, Inst Adv Res Chem Sci IAdChem, Madrid 28049, Spain - Author
See more

Abstract

Vanillin, a key flavor compound found in vanilla beans, is widely used in the food and pharmaceutical industries for its aromatic properties and potential therapeutic benefits. This study presents a comprehensive quantum chemical analysis to elucidate the interaction mechanisms of vanillin with CYP450 enzymes, with a focus on mechanism-based inactivation. Three potential inactivation pathways were evaluated: aldehyde deformylation, methoxy dealkylation, and acetal formation. Aldehyde deformylation was identified as the most energy-efficient, involving the removal of the aldehyde group from vanillin and leading to the formation of benzyne intermediates that could react with the iron porphyrin moiety of CYP450, potentially resulting in enzyme inactivation. Further investigation into the interactions of vanillin with CYP2E1 and CYP1A2 was conducted using molecular docking and molecular dynamics (MD) simulation. The docking analyses supported the findings from DFT studies, wherein vanillin revealed high binding affinities with the studied isozymes. Moreover, vanillin occupied the main binding site in both isozymes, as evidenced by the inclusion of the heme moiety in their binding mechanisms. Employing a 100 ns molecular dynamics simulation, we scrutinized the interaction dynamics between vanillin and the two isozymes of CYP450. The assessment of various MD parameters along with interaction energies revealed that vanillin exhibited stable trajectories and substantial energy stabilization during its interaction with both CYP450 isozymes. These insights can guide future research and ensure the safe application of vanillin, especially in scenarios where it may interact with CYP450 enzymes. Vanillin's biotransformation by CYP450 was studied, identifying aldehyde deformylation as energy-efficient pathway. Docking and MD simulations showed stable interactions with CYP2E1 and CYP1A2, suggesting potential food safety implications.
[+]

Keywords

1-aminobenzotriazoleBiologContinuumDeformylationDensity-functional thermochemistryDynamicsEfficientEnzymesInactivation

Quality index

Bibliometric impact. Analysis of the contribution and dissemination channel

The work has been published in the journal Organic & Biomolecular Chemistry due to its progression and the good impact it has achieved in recent years, according to the agency WoS (JCR), it has become a reference in its field. In the year of publication of the work, 2024 there are still no calculated indicators, but in 2023, it was in position 15/57, thus managing to position itself as a Q2 (Segundo Cuartil), in the category Chemistry, Organic. Notably, the journal is positioned en el Cuartil Q2 para la agencia Scopus (SJR) en la categoría Organic Chemistry.

Independientemente del impacto esperado determinado por el canal de difusión, es importante destacar el impacto real observado de la propia aportación.

Según las diferentes agencias de indexación, el número de citas acumuladas por esta publicación hasta la fecha 2026-01-14:

  • WoS: 29
  • Scopus: 27
[+]

Impact and social visibility

From the perspective of influence or social adoption, and based on metrics associated with mentions and interactions provided by agencies specializing in calculating the so-called "Alternative or Social Metrics," we can highlight as of 2026-01-14:

  • The use of this contribution in bookmarks, code forks, additions to favorite lists for recurrent reading, as well as general views, indicates that someone is using the publication as a basis for their current work. This may be a notable indicator of future more formal and academic citations. This claim is supported by the result of the "Capture" indicator, which yields a total of: 1 (PlumX).

It is essential to present evidence supporting full alignment with institutional principles and guidelines on Open Science and the Conservation and Dissemination of Intellectual Heritage. A clear example of this is:

[+]

Leadership analysis of institutional authors

This work has been carried out with international collaboration, specifically with researchers from: Egypt; Saudi Arabia.

There is a significant leadership presence as some of the institution’s authors appear as the first or last signer, detailed as follows: Last Author (LAMSABHI, AL MOKHTAR).

[+]

Awards linked to the item

This project was funded by Researchers Supporting Project number (RSPD2024R1078), King Saud University, Riyadh, Saudi Arabia. This work was carried out with support from the project PID2023-150717NB-I00 from the Ministerio de Ciencia, Innovacion y Universidades in Spain and the PRIES-CM project Ref: Y2020/EMT-6290 from the Comunidad Autonoma de Madrid. The authors would also like to thank the Centro de Computacion Cientifica of the UAM (CCC-UAM).
[+]