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. 2025 Feb 20;14(3):246.
doi: 10.3390/antiox14030246.

Untargeted Chemical Profile, Antioxidant, and Enzyme Inhibition Activity of Physalis angulata L. from the Peruvian Amazon: A Contribution to the Validation of Its Pharmacological Potential

Gabriel Vargas-Arana  1   2 , Alfredo Torres-Benítez  3 , José Erick Ortega-Valencia  4 , Claudia Merino-Zegarra  1 , Pilar Carranza-Rosales  5 , Mario J Simirgiotis  6
Affiliations

Untargeted Chemical Profile, Antioxidant, and Enzyme Inhibition Activity of Physalis angulata L. from the Peruvian Amazon: A Contribution to the Validation of Its Pharmacological Potential

Gabriel Vargas-Arana et al. Antioxidants (Basel). .

Abstract

Physalis angulata is a plant of great value in traditional medicine known for its content of bioactive compounds, such as physalins and withanolides, which possess diverse biological activities. In this study, the chemical profile, antioxidant activity, and enzyme inhibition capacity of aqueous and ethanolic extracts obtained from the root, stem, leaves, calyx, and fruits of P. angulata collected in Peru were evaluated. A total of forty-two compounds were detected in the extracts using UHPLC-ESI-QTOF-MS analysis. In vitro analyses revealed that leaf extracts contained the highest concentration of phenolic compounds, while leaf and fruit extracts showed the best results in FRAP, DPPH, and ABTS antioxidant tests; on the other hand, inhibition of AChE, BChE, α-glucosidase, and α-amylase enzymes was variable, but calyx and fruit extracts showed higher effectiveness. In silico analyses indicated that the compounds physagulin A, physagulin F, physagulide P, physalin B, and withaminimin showed stable interactions and favorable binding affinities with the catalytic sites of the enzymes studied. These results confirm the pharmacological potential of extracts and compounds derived from different organs of P. angulata, suggesting their promising use in treating diseases related to the central nervous system and metabolic syndrome.

Keywords: Physalis angulata; bioactive compounds; biological activity; extracts; therapeutic properties.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
(A) Bolsa mullaca plant (Physalis angulata). (B) Distribution of Physalis angulata (GBIF).
Figure 2
Figure 2
UHPLC-MS chromatograms: (a) ethanolic and (b) aqueous root extract; (c) ethanolic and (d) aqueous stem extract; (e) ethanolic and (f) aqueous leaf extract; (g) ethanolic and (h) aqueous calli extract; (i) ethanolic and (j) aqueous fruit extract.
Figure 3
Figure 3
Pharmacokinetic properties of compounds obtained from Physalis angulata calculated with Osiris Data Warrior software. Note: red color indicates that it does not comply with pharmacokinetic analysis and green color indicates that it complies with pharmacokinetic analysis.
Figure 4
Figure 4
Toxicity risk analysis of compounds obtained from Physalis angulata using the Osiris Data warrior software. Note: green color shows low toxic tendency and blue color shows high toxic tendency.
Figure 5
Figure 5
Molecular docking between Physalis angulata compounds and acetylcholinesterase (TcAChE). (A) Molecular docking of physagulin A and the enzyme acetylcholinesterase (TcAChE); (B) predominant molecular interactions of physagulin A and the enzyme acetylcholinesterase (TcAChE); (C) molecular docking of withaminimin and the enzyme acetylcholinesterase (TcAChE); (D) predominant molecular interactions of withaminimin and the enzyme acetylcholinesterase (TcAChE).
Figure 6
Figure 6
Molecular docking between Physalis angulata compounds and butyrylcholinesterase (hBuChE). (A) Molecular docking of physalin B and the enzyme butyrylcholinesterase (hBuChE); (B) predominant molecular interactions of physalin B and the enzyme butyrylcholinesterase (hBuChE); (C) molecular docking of withaminimin and the enzyme butyrylcholinesterase (hBuChE); (D) predominant molecular interactions of withaminimin and the enzyme butyrylcholinesterase (hBuChE).
Figure 7
Figure 7
Molecular docking between Physalis angulata compounds and α-amylase. (A) Molecular docking of physagulin A and the enzyme α-amylase; (B) predominant molecular interactions of physagulin A and the enzyme α-amylase; (C) molecular docking of physagulin F and the enzyme α-amylase; (D) predominant molecular interactions of physagulin F and the enzyme α-amylase.
Figure 8
Figure 8
Molecular docking between Physalis angulata compounds and α-glucosidase. (A) Molecular docking of physagulide P and the enzyme α-glucosidase; (B) predominant molecular interactions of physagulide P and the enzyme α-glucosidase; (C) molecular docking of physagulin A and the enzyme α-glucosidase; (D) predominant molecular interactions of physagulin A and the enzyme α-glucosidase.
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