Purification of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides of Molecular Docking Analysis and Antihypertensive Effect from Plant Seeds Hydrolysates
學生姓名:
陳禹辰
指導教授:
陳冠文
學 期:
112上
摘 要:
One of the major causes of death around the world today is cardiovascular disease (CVD), its risk factors include hypertension and high blood pressure. When angiotensin I is exposed to angiotensin I21 converting enzyme (ACE), resulting in the formation of angiotensin II causes blood pressure to rise. Seed protein has high nutritional value and can be used as a good source of natural plant protein and
bioactive peptides with ACE inhibitory activity. Hazelnut seed hydrolysate was purified by Ion-exchange chromatography, Gel filtration
chromatogram, Reverse phase high performance liquid chromatography and peptide identification, the C2 peak had the highest ACE inhibition rate (89.50%), and YLVR exhibited the highest ACE inhibitory activity (IC50 = 15.42 mM), it serve as an non-competitive ACE inhibitor. The strong inhibition of ACE by YLVR may be attributed to the formation of cation–pi interactions and hydrogen bonds. Finally, in vivo data showed that administration of YLVR significantly reduced SBP in SHRs. Peony seed hydrolysate was successfully purified and identified four novel ACEI peptides, and among which, HWS (IC50 = 1.50 mM) and VLSGF (IC50 = 0.63 mM) exhibited significant inhibition
activity on ACE. The inhibition type of VLSGF and HWS is competitive and mixed-type inhibition against ACE, respectively. Molecular docking results showed that VLSGF and HWS exhibit hydrogen bonds with ACE active site (S1 and S2). VLSGF and HWS could achieve hypotensive effect by simulating NO release through upregulation of intracellular eNOS expression, and inhibiting the production of ROS in Ang II stimulated endothelial cells. In conclusion, the purified peptides isolated from plant seed protein hydrolysates have potential antihypertensive properties which could potentially be used as functional food ingredients.
bioactive peptides with ACE inhibitory activity. Hazelnut seed hydrolysate was purified by Ion-exchange chromatography, Gel filtration
chromatogram, Reverse phase high performance liquid chromatography and peptide identification, the C2 peak had the highest ACE inhibition rate (89.50%), and YLVR exhibited the highest ACE inhibitory activity (IC50 = 15.42 mM), it serve as an non-competitive ACE inhibitor. The strong inhibition of ACE by YLVR may be attributed to the formation of cation–pi interactions and hydrogen bonds. Finally, in vivo data showed that administration of YLVR significantly reduced SBP in SHRs. Peony seed hydrolysate was successfully purified and identified four novel ACEI peptides, and among which, HWS (IC50 = 1.50 mM) and VLSGF (IC50 = 0.63 mM) exhibited significant inhibition
activity on ACE. The inhibition type of VLSGF and HWS is competitive and mixed-type inhibition against ACE, respectively. Molecular docking results showed that VLSGF and HWS exhibit hydrogen bonds with ACE active site (S1 and S2). VLSGF and HWS could achieve hypotensive effect by simulating NO release through upregulation of intracellular eNOS expression, and inhibiting the production of ROS in Ang II stimulated endothelial cells. In conclusion, the purified peptides isolated from plant seed protein hydrolysates have potential antihypertensive properties which could potentially be used as functional food ingredients.
20231011-專題討論-摘要-陳禹辰.pdf