魚類副產物之水解物中血管收縮素轉換酶 (ACE) 抑制胜肽之純化與分子對接分析
學生姓名:
陳禹辰
指導教授:
陳冠文
學期:
111下
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 I-converting enzyme (ACE), resulting in the formation of angiotensin II causes blood pressure to rise. Synthetic ACE inhibitors have side effects, so the search for active peptides that inhibit ACE from natural sources has received attention. Through enzyme inhibition kinetics and molecular docking to discover the underlying mechanisms that allow peptides to serve as potential antihypertensive agents. Atlantic salmon bones protein hydrolysates (SBPH) undergo ultrafiltration for further fractionation, it was found that the greatest ACE-inhibitory activity was achieved by a molecular weight lower than 0.65 kDa. The peptide in F7 fraction comprised eight amino acids FCLYELAR (IC50 on ACE = 0.033 mg/mL), it serve as an uncompetitive ACE inhibitor. In molecular docking process showed that FCLYELAR peptide bind to zinc ions, which lead to ACE inhibition. Shortfin scad waste hydrolysate (SWH) ultra-filtered peptide fraction (< 3 kDa) possessed the highest ACE inhibitory activity, followed by the fraction 14 by gel filtration, the amino acid sequence of RGVGPVPAA (IC50 on ACE = 0.20 mg/mL) was identified, it obtained acted as a competitive ACE inhibitor. The molecular docking studies showed that the SWH peptide exhibit hydrogen bonds with ACE active site. In conclusion, the purified peptides isolated from fish waste protein hydrolysates have potential antihypertensive properties which could potentially be used as functional food ingredients.
魚類副產物之水解物中血管收縮素轉換酶_(ACE)_抑制胜肽的純化與分子對接分析.pdf