藻類蛋白水解物中血管升壓素轉換酶 (ACE) 抑制胜肽之 分子對接分析及其抗高血壓的作用
學生姓名:
鄭筑軒
指導教授:
陳冠文
學期:
112下
摘 要:
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. Seaweed is a sustainable protein source in the production of peptide-based drugs and functional foods to prevent disease, especially cardiovascular diseases and diabetes. Pyropia pseudolinearis protein hydrolysates were purified by RP-HPLC and MALDI-TOF/MS/MS. The major peptide sequence LRM exhibited the highest ACE inhibitory activity (IC50 = 0.15
µM). Docking simulation analyses showed that three peptides were coordinated in the active site of the ACE. However, these peptides do not bind to the zinc ion, which may be the reason for their relatively low ACE inhibitory activity. Spirulina platensis protein hydrolysates (SPH)
were purified by SEC-HPLC and HPLC-MS. SPH were obtained for VTY (IC50 = 23.39 µM) and LGVP (IC50 = 45.76 µM) were with relatively low IC50 values against ACE. At the ACE active site in the presence of Zn (II), with binding energies of -6.48 kcal/mol and -5.57 kcal/mol,
respectively. The results of the docking simulation investigation suggested that VTY displayed a strong binding power to the active pocket S1 (Ala354, Glu384, and Tyr523) and S2 (Gln281, His513, and Tyr520) of ACE via hydrogen bonds, and LGVP only interacted with the S1 pocket (Ala354 and Tyr523). Gracilaria tenuistipitata microalgae was successfully purified and identify a novel peptide, MQDAITSVINAADVQGK exhibited significant inhibitory activity on ACE and an inhibition rate of 95.4%. In vivo data showed that peptide administration of significantly reduced systolic blood pressure (SBP) in SHRs. In conclusion, the purified peptides isolated from algae protein hydrolysates have potential antihypertensive effect which could potentially be used as functional food ingredients.
µM). Docking simulation analyses showed that three peptides were coordinated in the active site of the ACE. However, these peptides do not bind to the zinc ion, which may be the reason for their relatively low ACE inhibitory activity. Spirulina platensis protein hydrolysates (SPH)
were purified by SEC-HPLC and HPLC-MS. SPH were obtained for VTY (IC50 = 23.39 µM) and LGVP (IC50 = 45.76 µM) were with relatively low IC50 values against ACE. At the ACE active site in the presence of Zn (II), with binding energies of -6.48 kcal/mol and -5.57 kcal/mol,
respectively. The results of the docking simulation investigation suggested that VTY displayed a strong binding power to the active pocket S1 (Ala354, Glu384, and Tyr523) and S2 (Gln281, His513, and Tyr520) of ACE via hydrogen bonds, and LGVP only interacted with the S1 pocket (Ala354 and Tyr523). Gracilaria tenuistipitata microalgae was successfully purified and identify a novel peptide, MQDAITSVINAADVQGK exhibited significant inhibitory activity on ACE and an inhibition rate of 95.4%. In vivo data showed that peptide administration of significantly reduced systolic blood pressure (SBP) in SHRs. In conclusion, the purified peptides isolated from algae protein hydrolysates have potential antihypertensive effect which could potentially be used as functional food ingredients.
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