scholarly journals Two novel ACE inhibitory peptides isolated from longan seeds: purification, inhibitory kinetics and mechanisms

RSC Advances ◽  
2020 ◽  
Vol 10 (22) ◽  
pp. 12711-12720 ◽  
Author(s):  
Atthasith Nuchprapha ◽  
Supawee Paisansak ◽  
Papassara Sangtanoo ◽  
Piroonporn Srimongkol ◽  
Tanatorn Saisavoey ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Inhibition Mechanism ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory ◽  
Subsequent Identification

The isolation and subsequent identification of the two novel ACE-inhibitory peptides, ETSGMKPTEL, and ISSMGILVCL from the longan seeds were achieved. The inhibition mechanism was investigated by molecular docking.

scholarly journals Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

2020 ◽  
Vol 21 (3) ◽  
pp. 1059 ◽  
Author(s):  
Ruidan Wang ◽  
Xin Lu ◽  
Qiang Sun ◽  
Jinhong Gao ◽  
Lin Ma ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Docking ◽  
Ace Inhibition ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Simulated Gastrointestinal Digestion ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

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.

scholarly journals I dentification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste

2018 ◽  
Vol 18 (9) ◽  
pp. 682-691 ◽  
Author(s):  
Fatma Krichen ◽  
Assaâd Sila ◽  
Juliette Caron ◽  
Sabrine Kobbi ◽  
Naima Nedjar ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Protein Hydrolysates ◽  
Shrimp Waste ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

ACE inhibitory peptides derived from de-fatted lemon basil seeds: optimization, purification, identification, structure–activity relationship and molecular docking analysis

2020 ◽  
Vol 11 (9) ◽  
pp. 8161-8178
Author(s):  
Norhameemee Kheeree ◽  
Papassara Sangtanoo ◽  
Piroonporn Srimongkol ◽  
Tanatorn Saisavoey ◽  
Onrapak Reamtong ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Process Conditions ◽  
Inhibitory Peptide ◽  
Docking Analysis ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptide ◽  
Structure Activity ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory ◽  
Molecular Docking Analysis

The study determines optimized process conditions to maximize ACE inhibitory peptide production. The two novel hexa-peptides (LGRNLPPI and GPAGPAGL) from de-fatted lemon basil seeds (DLBS) was achieved.

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