Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 65, Issue 46, Pages 10020-10028Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.7b04043
Keywords
sericin hydrolysis; in silico prediction; LC-MS; ACE-I inhibitory peptides; molecular docking; inhibitory mechanism
Funding
- National Natural Science Foundation of China [31401629, 21666004, 21676059, 21606054]
- Natural Science Foundation of Guangxi Zhuang Autonomous Region, China [2016GXNSFAA380229, 2017JJG120005]
- Scientific Research Foundation of Guangxi University [XGZ130963]
- Innovation and Entrepreneurship Training Program of Guangxi Zhuang Autonomous Region [201610593169, 201710593185]
Ask authors/readers for more resources
Several novel peptides with high ACE-I inhibitory activity were successfully screened from sericin hydrolysate (SH) by coupling in silico and in vitro approaches for the first time. Most screening processes for ACE-I inhibitory peptides were achieved through high-throughput in silico simulation followed by in vitro verification. QSAR model based predicted results indicated that the ACE-I inhibitory activity of these SH peptides and six chosen peptides exhibited moderate high ACE-I inhibitory activities (log IC50 values: 1.63-2.34). Moreover, two tripeptides among the chosen six peptides were selected for ACE-I inhibition mechanism analysis which based on Lineweaver-Burk plots indicated that they behave as competitive ACE-I inhibitors. The C-terminal residues of short-chain peptides that contain more H-bond acceptor groups could easily form hydrogen bonds with ACE-I and have higher ACE-I inhibitory activity. Overall, sericin protein as a strong ACE-I inhibition source could be deemed a promising agent for antihypertension applications.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available