Angiotensin I–Converting Enzyme Inhibitory Activity of Peptides Derived from Egg White Proteins by Enzymatic Hydrolysis

2004 ◽  
Vol 67 (9) ◽  
pp. 1914-1920 ◽  
Author(s):  
M. MIGUEL ◽  
I. RECIO ◽  
J. A. GÓMEZ-RUIZ ◽  
M. RAMOS ◽  
R. LÓPEZ-FANDIÑO
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Molecular Mass ◽  
Inhibitory Activity ◽  
High Performance ◽  
Egg White ◽  
Reversed Phase ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

The hydrolysis of crude egg white with pepsin, trypsin, and chymotrypsin produced peptides with angiotensin-converting enzyme (ACE) inhibitory properties. These peptides were mainly derived from the proteolysis of ovalbumin. The most active hydrolysates were obtained after treatment with pepsin (50% inhibitory concentration [IC50], 55.3 μg/ml), with the fraction having a molecular mass lower than 3,000 Da giving the highest ACE inhibitory activity (IC50, 34.5 μg/ml). Nine subfractions were collected from the fraction with a molecular mass lower than 3,000 Da using semipreparative reversed-phase high-performance liquid chromatography. Considerable ACE inhibitory activity (IC50 < 40 μg/ml) was found in three of them. These subfractions were analyzed by reversed-phase high-performance liquid chromatography–tandem mass spectrometry, and 14 peptides were identified. These sequences were synthesized, and their ACE inhibitory activities were measured. Among the identified peptides, two novel sequences with potent ACE inhibitory activity were found. The amino acid sequences of these inhibitors were identified as Arg-Ala-Asp-His-Pro-Phe-Leu and Tyr-Ala-Glu-Glu-Arg-Tyr-Pro-Ile-Leu and showed IC50 values of 6.2 and 4.7 μM, respectively.

scholarly journals Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

Marine Drugs ◽  
2018 ◽  
Vol 16 (11) ◽  
pp. 411 ◽  
Author(s):  
Fangmiao Yu ◽  
Zhuangwei Zhang ◽  
Liwang Luo ◽  
Junxiang Zhu ◽  
Fangfang Huang ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Molecular Docking ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Cyclina Sinensis ◽  
Ace Inhibitory

Marine-derived angiotensin-I converting enzyme (ACE) inhibitory peptides have shown potent ACE inhibitory activity with no side effects. In this study, we reported the discovery of a novel ACE-inhibitory peptide derived from trypsin hydrolysates of Cyclina sinensis (CSH). CSH was separated into four different molecular weight (MW) fractions by ultrafiltration. Fraction CSH-I showed the strongest ACE inhibitory activity. A peptide was purified by fast protein liquid chromatography (FPLC) and reversed-phase high-performance liquid chromatography (RP-HPLC) and its sequence was determined to be Trp-Pro-Met-Gly-Phe (WPMGF, 636.75 Da). The Lineweaver-Burk plot showed that WPMGF was a competitive inhibitor of ACE. WPMGF showed a significant degree of stability at varying temperatures, pH, and simulated gastrointestinal environment conditions. We investigated the interaction between this pentapeptide and ACE by means of a flexible molecular docking tool. The results revealed that effective interaction between WPMGF and ACE occurred mainly through hydrogen bonding, hydrophobic interactions, and coordination bonds between WPMGF and Zn(II). In conclusion, our study indicates that a purified extract derived from Cyclina sinensis or the WPMGF peptide could potentially be incorporated in antihypertensive functional foods or dietary supplements.

scholarly journals Screening of Angiotensin-I Converting Enzyme Inhibitory Peptides Derived from Caulerpa lentillifera

Molecules ◽  
2018 ◽  
Vol 23 (11) ◽  
pp. 3005 ◽  
Author(s):  
Cesarea Joel ◽  
Christoper Sutopo ◽  
Arief Prajitno ◽  
Jui-Hsin Su ◽  
Jue-Liang Hsu
Keyword(s):  
Liquid Chromatography ◽  
Inhibitory Activity ◽  
Antihypertensive Agents ◽  
Docking Simulation ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Caulerpa Lentillifera ◽  
Ace Inhibitory

Peptides with angiotensin-I converting enzyme (ACE) inhibitory activity have received considerable interest due to their potential as antihypertensive agents and consumer concern over the safety of synthetic drugs. The objective of this study was to isolate ACE inhibitory (ACEI) peptides from Caulerpa lentillifera (known commonly as sea grape) protein hydrolysate. In this study, short-chain peptides were obtained after hydrolysis by various enzymes and subsequently by ultrafiltration. Thermolysin hydrolysate showed the highest ACEI activity. Bioassay-guided fractionation was performed using reversed-phase high performance liquid chromatography (RP-HPLC) to uncover the fraction 9 with the highest ACE inhibitory activity from thermolysin hydrolysate. Peptides in this fraction were further identified using liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis coupled with de novo sequencing, which gave two oligopeptides, FDGIP (FP-5) and AIDPVRA (AA-7). The identities and activities of these two peptides were further confirmed using synthetic peptides. Their IC50 values were determined as 58.89 ± 0.68 µM and 65.76 ± 0.92 µM, respectively. Moreover, the inhibition kinetics revealed that both FP-5 and AA-7 are competitive inhibitors. These activities were further explained using molecular docking simulation. The present study is the first report about ACEI peptides derived from Caulerpa lentillifera and it shows the potential for preventing hypertension and for functional food development.

Assessment and Separation of Angiotensin I-Converting Enzyme Inhibitory Peptides in Chinese Soypaste

2015 ◽  
Vol 11 (2) ◽  
pp. 301-305 ◽  
Author(s):  
Fengjuan Li ◽  
Kohji Yamaki ◽  
Yongqiang Cheng ◽  
Yuanyuan Fang
Keyword(s):  
Inhibitory Activity ◽  
Reversed Phase ◽  
Substantial Contribution ◽  
Spectrometric Analysis ◽  
Dependent Manner ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Abstract A Chinese soypaste-derived fraction with potent angiotensin I-converting enzyme (ACE) inhibitory activity (IC50 = 25.9 μg/mL) was obtained by treating soypaste extract with 80% ethanol. The result of gradient reversed-phase high-performance liquid chromatography (RP-HPLC) suggested that bioactive peptides bearing some polarity groups made a substantial contribution to the ACE inhibitory activity. By mass spectrometric analysis, a component was separated as Glu-Ser-Gly-Asp which was then found to act in a dose-dependent manner against ACE activity as a non-competitive inhibitor, with an IC50 value of 2.297 mM.

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