scholarly journals Identification and molecular docking of novel α-glucosidase inhibitory peptides from hydrolysates of Betel River buffalo casein

LWT ◽  
2022 ◽  
pp. 113062
Author(s):  
Qiong Zhao ◽  
Guangqiang Wei ◽  
Kunling Li ◽  
Shihong Duan ◽  
Rong Ye ◽  
...  
2021 ◽  
Vol 353 ◽  
pp. 129471
Author(s):  
Yan-xia Feng ◽  
Zi-chun Wang ◽  
Jia-xin Chen ◽  
Hai-rong Li ◽  
Yan-bing Wang ◽  
...  

2020 ◽  
Vol 21 (3) ◽  
pp. 1059 ◽  
Author(s):  
Ruidan Wang ◽  
Xin Lu ◽  
Qiang Sun ◽  
Jinhong Gao ◽  
Lin Ma ◽  
...  

The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (< 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest™ 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 ± 0.10 μM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.


2018 ◽  
Vol 9 (1) ◽  
pp. 594-603 ◽  
Author(s):  
Chan Zhong ◽  
Le-Chang Sun ◽  
Long-Jie Yan ◽  
Yi-Chen Lin ◽  
Guang-Ming Liu ◽  
...  

The purification, characterization, and molecular docking study of a novel ACE inhibitory peptide (NAPHMR) derived from sea cucumber gonad hydrolysates.


2014 ◽  
Vol 60 (1) ◽  
pp. 92-98 ◽  
Author(s):  
Ahmad Asoodeh ◽  
Leyla Haghighi ◽  
Jamashidkhan Chamani ◽  
Mohamad Amin Ansari-Ogholbeyk ◽  
Zahra Mojallal-Tabatabaei ◽  
...  

2018 ◽  
Author(s):  
Shehu Muhammad Auwal ◽  
Najib Zainal Abidin ◽  
Mohammad Zarei ◽  
Chin Ping Tan ◽  
Nazamid Saari

AbstractStone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated based on hydrophobicity and isoelectric properties of the constituent peptides. Five novel peptide sequences with molecular weight (mw) < 1000 daltons (Da) were identified using LC-MS/MS. The peptides including ALGPQFY (794.44 Da), KVPPKA (638.88 Da), LAPPTM (628.85 Da), EVLIQ (600.77 Da) and EHPVL (593.74 Da) were evaluated for ACE-inhibitory activity and showed IC50 values of 0.012 mM, 0.980 mM, 1.31 mM, 1.44 mM and 1.68 mM, respectively. The ACE-inhibitory effects of the peptides were further verified using molecular docking study. The docking results demonstrated that the peptides exhibit their effect mainly via hydrogen and electrostatic bond interactions with ACE. These findings provide evidence about stone fish as a valuable source of raw materials for the manufacture of antihypertensive peptides that can be incorporated to enhance therapeutic relevance and commercial significance of formulated functional foods.


Sign in / Sign up

Export Citation Format

Share Document