Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides of Molecular Docking Analysis and Antihypertensive Effect of Fish By3 Products Hydrolysates

學生姓名: 鄭筑軒
指導教授: 陳冠文
學期: 113上
摘  要: As about 18 million patients die from cardiovascular disease every year,accounting for approximately one-third of global deaths. ACE, a component of the renin-angiotensin system, is a zinc metalloprotease that catalyzes cleavage of the C terminal dipeptide from Ang I to produce the potent vasopressor octapeptide Ang II. The search for safer drugs from fish by- products can offer a viable alternative to chemosynthetic drugs for lowering high blood pressure Katsuwonus pelamis protein hydrolysate were purified by GPC and RP-HPLC. The major peptide sequence ICY
exhibited the highest ACE inhibitory activity (IC50 = 0.48 µM). Oreochromis mossambicus protein hydrolyzate were purified by gel filtration chromatography and UPLC-MS/MS. The results were obtained for VGLFPSRSF (IC50 = 61.43 μM) were with relatively low IC50 values against ACE. Decapterus macrosoma protein hydrolysate was successfully purified and identify a novel peptide, RGVGPVPAA (IC50 = 2.20 mg/mL). In conclusion, the purified peptides isolated from fish by-products protein hydrolysates have potential antihypertensive effects which could potentially be
used as functional food ingredients.