Antihypertensive Effects, Molecular Docking Study, and Isothermal Titration Calorimetry Assay of Angiotensin I-Converting Enzyme Inhibitory Peptides fromChlorella vulgaris

2018 ◽  
Vol 66 (6) ◽  
pp. 1359-1368 ◽  
Author(s):  
Jingli Xie ◽  
Xujun Chen ◽  
Junjie Wu ◽  
Yanyan Zhang ◽  
Yan Zhou ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Isothermal Titration Calorimetry ◽  
Docking Study ◽  
Titration Calorimetry ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Molecular Docking Study ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme

Potential angiotensin I converting enzyme inhibitory peptides from gluten hydrolysate: Biochemical characterization and molecular docking study

2014 ◽  
Vol 60 (1) ◽  
pp. 92-98 ◽  
Author(s):  
Ahmad Asoodeh ◽  
Leyla Haghighi ◽  
Jamashidkhan Chamani ◽  
Mohamad Amin Ansari-Ogholbeyk ◽  
Zahra Mojallal-Tabatabaei ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Biochemical Characterization ◽  
Docking Study ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Molecular Docking Study ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme

Production, optimisation and characterisation of angiotensin converting enzyme inhibitory peptides from sea cucumber (Stichopus japonicus) gonad

2018 ◽  
Vol 9 (1) ◽  
pp. 594-603 ◽  
Author(s):  
Chan Zhong ◽  
Le-Chang Sun ◽  
Long-Jie Yan ◽  
Yi-Chen Lin ◽  
Guang-Ming Liu ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Sea Cucumber ◽  
Docking Study ◽  
Converting Enzyme ◽  
Molecular Docking Study ◽  
Inhibitory Peptide ◽  
Stichopus Japonicus ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptide ◽  
Ace Inhibitory

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

scholarly journals Identification, structure-activity relationship and in silico molecular docking analyses of five novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from stone fish hydrolysates

2018 ◽  
Author(s):  
Shehu Muhammad Auwal ◽  
Najib Zainal Abidin ◽  
Mohammad Zarei ◽  
Chin Ping Tan ◽  
Nazamid Saari
Keyword(s):  
Molecular Docking ◽  
Raw Materials ◽  
Docking Study ◽  
Inhibitory Effects ◽  
Molecular Docking Study ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
In Silico Molecular Docking ◽  
Ace Inhibitory ◽  
Antihypertensive Peptides

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.

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