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Kinetics of the Inhibition of Renin and Angiotensin I Converting Enzyme by Polar and Non-polar Polyphenolic Extracts of <Emphasis Type="Italic">Vernonia Amygdalina</Emphasis> and <Emphasis Type="Italic">Gongronema Latifolium</Emphasis> Leaves
Authors:Comfort F Ajibola  Afolabi F Eleyinmi  Rotimi E Aluko
Institution:(1) Department of Food Science and Technology, Federal University of Technology, PMB 704 Akure, Nigeria;(2) Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, MB, R3T 2N2, Canada;(3) Human Resources and Skill Development, Edmonton, AB, Canada;(4) The Richardson Centre for Functional Foods and Nutraceuticals, University of Manitoba, Winnipeg, MB, Canada;
Abstract:The aim of this study was to determine the in vitro modulation of the renin-angiotensin system by polyphenolic extracts and fractions of two green leafy vegetables, Vernonia amygdalina (VA) and Gongronema latifolium (GL), that are used for food and medicinal purposes. An 80% acetone extract of each leaf was fractionated on silicic acid-packed column to give two main fractions: acetone eluate (flow-through) and ethanol eluate (column-bound), that consist mostly of chlorophyllic and non-chlorophyllic fractions, respectively. Column fractionation resulted in polyphenolic fractions that displayed higher potency against angiotensin converting enzyme (ACE) and renin than the crude acetone extracts; generally, the chlorophyllic fraction was more active than the non-chlorophyllic fraction. ACE-inhibitory activity was significantly higher (p < 0.05) for the chlorophyllic fraction of VA than GL, with IC50 values of 0.207 and 0.413 mg/ml, respectively. Similarly, the chlorophyllic fraction of VA had significantly higher (p < 0.05) renin inhibition than GL, with IC50 values of 0.172 and 0.513 mg/ml, respectively. Kinetics studies showed that the chlorophyllic fractions of VA and GL exhibited mostly mixed-type ACE and renin inhibitions. We concluded that the hydrophobic nature of the chlorophyllic fraction may have contributed to the increased interaction with enzyme protein and inhibition of activities of ACE and renin.
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