源自发酵米糠的新型血管紧张素转换酶和胰脂肪酶寡肽抑制剂。
Novel angiotensin-converting enzyme and pancreatic lipase oligopeptide inhibitors from fermented rice bran.
作者信息
Hu Jingfei, Wang Huanyu, Weng Nanhai, Wei Tong, Tian Xueqing, Lu Jing, Lyu Mingsheng, Wang Shujun
机构信息
Jiangsu Key Laboratory of Marine Bioresources and Environment, Jiangsu Ocean University, Lianyungang, China.
Jiangsu Key Laboratory of Marine Biotechnology, Jiangsu Ocean University, Lianyungang, China.
出版信息
Front Nutr. 2022 Sep 15;9:1010005. doi: 10.3389/fnut.2022.1010005. eCollection 2022.
This study determined the inhibitory activity of oligopeptides against angiotensin-converting enzyme (ACE) and pancreatic lipase through tests, molecular docking, and enzyme inhibition. The results showed that the IC of GLLGY, HWP, and VYGF for ACE inhibition was 1 mg/mL, and the IC of HWP for pancreatic lipase was 3.95 mg/mL. Molecular docking revealed that the binding energies between GLLGY, HWP, and VYGF and ACE were -9.0, -8.4, and -9.2 kcal/mol, respectively. The binding free energy between HWP and pancreatic lipase was -7.3 kcal/mol. GLLGY, HWP, and VYGF inhibited ACE compentitively. HWP inhibited pancreatic lipase through non-competition. simulated gastrointestinal digestion, the three oligopeptides still had inhibitory activity and low toxicity. The results revealed that the peptides GLLGY, HWP, and VYGF may be suitable candidates for further research on ACE inhibition, and HWP may be a suitable candidate for studying pancreatic lipase inhibition.
本研究通过实验、分子对接和酶抑制法测定了寡肽对血管紧张素转换酶（ACE）和胰脂肪酶的抑制活性。结果表明，GLLGY、HWP和VYGF对ACE抑制的IC50为1 mg/mL，HWP对胰脂肪酶的IC50为3.95 mg/mL。分子对接显示，GLLGY、HWP和VYGF与ACE之间的结合能分别为-9.0、-8.4和-9.2 kcal/mol。HWP与胰脂肪酶之间的结合自由能为-7.3 kcal/mol。GLLGY、HWP和VYGF竞争性抑制ACE。HWP通过非竞争性方式抑制胰脂肪酶。经模拟胃肠道消化后，这三种寡肽仍具有抑制活性且毒性较低。结果表明，肽GLLGY、HWP和VYGF可能是进一步研究ACE抑制的合适候选物，而HWP可能是研究胰脂肪酶抑制的合适候选物。
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