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Review
. 2023 May 12:10:1177897.
doi: 10.3389/fnut.2023.1177897. eCollection 2023.

Role of flavonoids in controlling obesity: molecular targets and mechanisms

Anns Mahboob  1 , Samson Mathews Samuel  2 , Arif Mohamed  3 , Mohmmad Younus Wani  3 , Sofiane Ghorbel  4 , Nabil Miled  3 , Dietrich Büsselberg  2 , Ali Chaari  1
Affiliations
Review

Role of flavonoids in controlling obesity: molecular targets and mechanisms

Anns Mahboob et al. Front Nutr. .

Abstract

Obesity presents a major health challenge that increases the risk of several non-communicable illnesses, such as but not limited to diabetes, hypertension, cardiovascular diseases, musculoskeletal and neurological disorders, sleep disorders, and cancers. Accounting for nearly 8% of global deaths (4.7 million) in 2017, obesity leads to diminishing quality of life and a higher premature mortality rate among affected individuals. Although essentially dubbed as a modifiable and preventable health concern, prevention, and treatment strategies against obesity, such as calorie intake restriction and increasing calorie burning, have gained little long-term success. In this manuscript, we detail the pathophysiology of obesity as a multifactorial, oxidative stress-dependent inflammatory disease. Current anti-obesity treatment strategies, and the effect of flavonoid-based therapeutic interventions on digestion and absorption, macronutrient metabolism, inflammation and oxidative stress and gut microbiota has been evaluated. The use of several naturally occurring flavonoids to prevent and treat obesity with a long-term efficacy, is also described.

Keywords: anti-obesity therapy; flavonoids; metabolic syndrome; natural compounds; obesity.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
ROS generating pathways in obesity and related complications/diseases.
Figure 2
Figure 2
Quercetin chemical structure showing chemical determinants for flavonoid binding to glucosidase (51).
Figure 3
Figure 3
Structure of the pancreatic α-amylase complex with myricetin and ethyl caffeate (pdb code 4 W93). (A) The phenolic compounds within the catalytic pocket of the enzyme. (B) Interacting residues with phenolic compounds are displayed as sticks, and hydrogen bonding is shown as dotted lines. The figure was constructed using the BIOVIA Discovery Studio software (BIOVIA, Dassault Systèmes, [BIOVIA Discovery Studio], [v17.2.0.16349], San Diego: Dassault Systèmes, [2017]).
Figure 4
Figure 4
Docking models of pancreatic lipase with quercetin and myricetin. (A) The quercetin (green) and myricetin (orange) are superimposed and presented as sticks. (B) Interacting residues with quercetin in the lipase active site. (C) Interacting residues with myricetin in the lipase active site. Pancreatic lipase, quercetin, and myricetin structures were extracted from pdb structures with codes 1ETH, 6TTC, and 7VUM, respectively. Docking was carried out using autodock Vina software with a radius of 1.00, the center coordinates x: 64, y = 38.953 and z = 133.121, and a box size of 40. The figure was constructed using the BIOVIA Discovery Studio software (BIOVIA, Dassault Systèmes, [BIOVIA Discovery Studio], [v17.2.0.16349], San Diego: Dassault Systèmes, [2017]).
See this image and copyright information in PMC

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