Evaluation of the osteoprotective potential of whey derived-antioxidative (YVEEL) and angiotensin-converting enzyme inhibitory (YLLF) bioactive peptides in ovariectomised rats

2018 ◽  
Vol 9 (9) ◽  
pp. 4791-4801 ◽  
Author(s):  
Masum Pandey ◽  
Suman Kapila ◽  
Rajeev Kapila ◽  
Ritu Trivedi ◽  
Anirudh Karvande
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Bioactive Peptides ◽  
Converting Enzyme ◽  
Inhibitory Peptide ◽  
Ace Inhibitory Peptide ◽  
Antioxidative Peptide ◽  
Ace Inhibitory ◽  
Ovariectomised Rats

Whey-derived antioxidative peptide showed an enhanced osteoprotective effect as compared to ACE inhibitory peptide.

Studies on the Interaction between Angiotensin-Converting Enzyme (ACE) and ACE Inhibitory Peptide from Saurida elongata

2018 ◽  
Vol 66 (51) ◽  
pp. 13414-13422 ◽  
Author(s):  
Xiongdiao Lan ◽  
Lixia Sun ◽  
Yaseen Muhammad ◽  
Zefen Wang ◽  
Haibo Liu ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Converting Enzyme ◽  
Inhibitory Peptide ◽  
Ace Inhibitory Peptide ◽  
Ace Inhibitory

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 A Novel Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptide from Takifugu flavidus

Marine Drugs ◽  
2021 ◽  
Vol 19 (12) ◽  
pp. 651
Author(s):  
Yongchang Su ◽  
Shicheng Chen ◽  
Shuilin Cai ◽  
Shuji Liu ◽  
Nan Pan ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Inhibitory Activity ◽  
Gel Chromatography ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Ace Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Alcalase, neutral protease, and pepsin were used to hydrolyze the skin of Takifugu flavidus. The T. flavidus hydrolysates (TFHs) with the maximum degree of hydrolysis (DH) and angiotensin-I-converting enzyme (ACE)-inhibitory activity were selected and then ultra-filtered to obtain fractions with components of different molecular weights (MWs) (<1, 1–3, 3–10, 10–50, and >50 kDa). The components with MWs < 1 kDa showed the strongest ACE-inhibitory activity with a half-maximal inhibitory concentration (IC50) of 0.58 mg/mL. Purification and identification using semi-preparative liquid chromatography, Sephadex G-15 gel chromatography, RP-HPLC, and LC–MS/MS yielded one new potential ACE-inhibitory peptide, PPLLFAAL (non-competitive suppression mode; IC50 of 28 μmmol·L−1). Molecular docking and molecular dynamics simulations indicated that the peptides should bind well to ACE and interact with amino acid residues and the zinc ion at the ACE active site. Furthermore, a short-term assay of antihypertensive activity in spontaneously hypertensive rats (SHRs) revealed that PPLLFAAL could significantly decrease the systolic blood pressure (SBP) and diastolic blood pressure (DBP) of SHRs after intravenous administration. These results suggested that PPLLFAAL may have potential applications in functional foods or pharmaceuticals as an antihypertensive agent.

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