Key result
Herbal CJI extracts demonstrate in vitro antioxidant activity and strong in silico RAAS target binding.
Why the study?
The combination of Centella asiatica leaves, Justicia gendarussa leaves, and Imperata cylindrica roots is used to treat hypertension, requiring identification of its blood pressure-lowering bioactive compounds and their mechanisms against renin-angiotensin-aldosterone system protein targets.
Do bioactive compounds from the herbal combination of Centella asiatica, Justicia gendarussa, and Imperata cylindrica exhibit in vitro antioxidant activity and in silico binding affinity to inhibit RAAS protein targets (renin, ACE, AT1R, MR)?
Do bioactive compounds from the herbal combination of Centella asiatica, Justicia gendarussa, and Imperata cylindrica exhibit in vitro antioxidant activity and in silico binding affinity to inhibit RAAS protein targets (renin, ACE, AT1R, MR)?
Bioactive compounds from the traditional herbal combination of Centella asiatica, Justicia gendarussa, and Imperata cylindrica demonstrate in vitro antioxidant properties and strong in silico binding affinities to multiple RAAS protein targets (renin, ACE, AT1R, and MR), providing a preclinical basis for potential multitarget antihypertensive investigation.
Answers are grounded in this paper and cite their sources.
Preclinical only; leaves open whether these bioactives yield antihypertensive effects in vivo.
Background: Hypertension is a leading global health challenge. It has been a major risk factor for cardiovascular disease events that contribute broadly to morbidity and mortality worldwide. With increasing life expectancy and changes in lifestyle and diet, the prevalence of hypertension has increased by up to 40% in certain parts of Asia, particularly in low- and middle-income countries (LMICs). The combination of Centella asiatica (C) leaves, Justicia gandarussa (J) leaves, and Imperata cylindrica (I) roots has been used to treat hypertension. Objective: To identify potential active substances that lower blood pressure, bioactive compounds from CJI were isolated and characterized in vitro, and in silico predictions were generated. Active compounds were identified with LC-HRMS. Methods: We hypothesized that the active compounds of CJI act as multitarget antihypertensives by inhibiting protein targets in the renin-angiotensin-aldosterone system (RAAS), including aspartic proteinase renin (2V0Z), Angiotensin-Converting Enzyme (ACE, 1R4L), angiotensin receptor (AT1R), and mineralocorticoid receptor (MR, 2AA2). LC-HRMS analysis identified 42 active compounds from CJI. Results: Ethanol extract of CJI showed antioxidant activity with an IC50 of 187,866 ppm. Our results indicated that various active substances in CJI could bind to different drug targets. For renin, cylindrin, and friedelin, binding affinities of -11 and -10.2 kcal/mol were observed at the S3 binding site, potentially blocking renin activity. For ACE, castillicetin and 1,5-dicaffeoylquinic acid exhibited binding affinities of -10.5 and -10.4 kcal/mol, respectively, and bound to its binding pocket. For AT1R, fernenol and friedelin had binding affinities of around -11 kcal/mol within the binding pocket. Regarding MR, only cylindrin could bind, with an affinity of -8.8 kcal/mol. Conclusion: the CJI combination shows promise as an alternative treatment for hypertension, likely inhibiting multiple drug targets in the RAAS pathway.
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Sulistyowati et al. (2026) studied Hypertension. Ethanol extract and bioactive compounds from Centella asiatica, Justicia gendarussa, and Imperata cylindrica (CJI combination) vs. Ascorbic acid (antioxidant control) and standard RAAS inhibitors (benazepril-HCl, olmesartan, valsartan, spironolactone, eplerenone) was evaluated on In vitro DPPH antioxidant activity (IC50) and in silico binding affinity (kcal/mol) to RAAS protein targets (Renin 2V0Z, ACE 1R4L, AT1R 4ZUD, and MR 2AA2). Bioactive compounds from Centella asiatica, Justicia gendarussa, and Imperata cylindrica showed in vitro antioxidant activity (IC50 187.866 ppm) and strong in silico binding to RAAS targets.
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