Screening, discovery, and characterization of angiotensin-I converting enzyme inhibitory peptides derived from proteolytic hydrolysate of bitter melon seed proteins

Priyanto, Anugerah Dany; Doerksen, Robert J.; Chang, Ching‐Cheng; Sung, Wang-Chou; Widjanarko, Simon Bambang; Kusnadi, Joni; Lin, Ya-Chi; Wang, Ting-Chin; Hsu, Jue‐Liang

doi:10.1016/j.jprot.2015.08.018

Cited by 79 publications

(73 citation statements)

References 59 publications

(62 reference statements)

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“…Authors used docking to study interactions between RYL and its target. In other work, Priyanto et al [25] identified new ACE inhibitory peptides (VY-7 and VG-8) from a thermolysin digest of bitter melon (Momordica charantia) seed proteins. They used docking to study the orientation and chemical interactions of these peptides forming complexes with ACE.…”

Section: Molecular Modeling Applied To the Study Of Ace Inhibitors Inmentioning

confidence: 99%

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

Caballero

2020

Molecules

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The angiotensin-converting enzyme (ACE) is a two-domain dipeptidylcarboxypeptidase, which has a direct involvement in the control of blood pressure by performing the hydrolysis of angiotensin I to produce angiotensin II. At the same time, ACE hydrolyzes other substrates such as the vasodilator peptide bradykinin and the anti-inflammatory peptide N-acetyl-SDKP. In this sense, ACE inhibitors are bioactive substances with potential use as medicinal products for treatment or prevention of hypertension, heart failures, myocardial infarction, and other important diseases. This review examined the most recent literature reporting ACE inhibitors with the help of molecular modeling. The examples exposed here demonstrate that molecular modeling methods, including docking, molecular dynamics (MD) simulations, quantitative structure-activity relationship (QSAR), etc, are essential for a complete structural picture of the mode of action of ACE inhibitors, where molecular docking has a key role. Examples show that too many works identified ACE inhibitory activities of natural peptides and peptides obtained from hydrolysates. In addition, other works report non-peptide compounds extracted from natural sources and synthetic compounds. In all these cases, molecular docking was used to provide explanation of the chemical interactions between inhibitors and the ACE binding sites. For docking applications, most of the examples exposed here do not consider that: (i) ACE has two domains (nACE and cACE) with available X-ray structures, which are relevant for the design of selective inhibitors, and (ii) nACE and cACE binding sites have large dimensions, which leads to non-reliable solutions during docking calculations. In support of the solution of these problems, the structural information found in Protein Data Bank (PDB) was used to perform an interaction fingerprints (IFPs) analysis applied on both nACE and cACE domains. This analysis provides plots that identify the chemical interactions between ligands and both ACE binding sites, which can be used to guide docking experiments in the search of selective natural components or novel drugs. In addition, the use of hydrogen bond constraints in the S2 and S2′ subsites of nACE and cACE are suggested to guarantee that docking solutions are reliable.

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Section: Molecular Modeling Applied To the Study Of Ace Inhibitors Inmentioning

confidence: 99%

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

Caballero

2020

Molecules

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“…Regardless of the enzyme used, temperature, hydrolysis time, and enzyme to protein ratio are considered crucial factors in the production of peptide with ACE-inhibitory activity [10,26,35,51]. Due to the specificity of the proteolytic enzyme to substrate, the peptide composition of hydrolysates, and therefore ACE-inhibitory activities change [52,53].…”

Section: Production Of Ace-inhibitory Peptides From Plantsmentioning

confidence: 99%

“…The stability and absorption of the peptides obtained from bitter melon seed proteins during gastrointestinal digestion were simulated using pepsin and trypsin enzymes by Priyanto et al [26]. It has been reported that the stability of the peptides differed depending on the simulated gastrointestinal digestion.…”

Section: Bioavailability Of Ace Inhibitor Peptidesmentioning

confidence: 99%

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

et al. 2017

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Hypertension is an important factor in cardiovascular diseases. Angiotensin-I-converting enzyme (ACE) inhibitors like synthetic drugs are widely used to control hypertension. ACE-inhibitory peptides from food origins could be a good alternative to synthetic drugs. A number of plant-based peptides have been investigated for their potential ACE inhibitor activities by using in vitro and in vivo assays. These plant-based peptides can be obtained by solvent extraction, enzymatic hydrolysis with or without novel food processing methods, and fermentation. ACE-inhibitory activities of peptides can be affected by their structural characteristics such as chain length, composition and sequence. ACE-inhibitory peptides should have gastrointestinal stability and reach the cardiovascular system to show their bioactivity. This paper reviews the current literature on plant-derived ACE-inhibitory peptides including their sources, production and structure, as well as their activity by in vitro and in vivo studies and their bioavailability.

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“…), hen egg white lysozyme hydrolysate (Rao et al . ), melon seed protein hydrolysates (Priyanto et al ). Nevertheless, the K i values reported in the present studies were much lower than those reported for ACE inhibitory F3 peptides isolated from ostrich egg white (Tanzadehpanah et al .…”

Section: Resultsmentioning

confidence: 99%

Purification and identification of Ace-inhibitory peptides from poultry viscera protein hydrolysate

Mane

Jamdar

2016

Journal of Food Biochemistry

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Three novel Angiotensin I‐converting enzyme (ACE) inhibitory peptides were isolated from poultry viscera protein hydrolysate (PVPH). The purification steps involved ultrafiltration of PVPH to eliminate the high molecular weight peptides and RP‐HPLC. The ACE inhibitory activity was resolved into three peaks on C18 column with retention times of 15.0, 18.9 and 20.9 min and amino acid sequences of the three peptides were determined to be ARIYH, LRKGNLE and RVWCP, respectively. The peptides exhibited resistance to hydrolysis by gastrointestinal proteases and extreme temperature (100C) and pH (1–12) at least for 2 h. Two of these peptides were competitive inhibitors, while the third was noncompetitive. The in vitro ACE inhibitory activity of PVPH revealed it could be a promising economic source for nutraceutical applications. Practical Applications Poultry viscera is a protein‐rich by‐product of poultry processing industry. The tissue protein and its hydrolysate offer huge potential for different bioactive peptides. In the present study three novel ACE inhibitory peptides were identified and characterized from poultry viscera protein hydrolysate (PVPH). These peptides could be tested further for their in vivo antihypertensive effect and as functional ingredient in foods.

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Screening, discovery, and characterization of angiotensin-I converting enzyme inhibitory peptides derived from proteolytic hydrolysate of bitter melon seed proteins

Cited by 79 publications

References 59 publications

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

Purification and identification of Ace-inhibitory peptides from poultry viscera protein hydrolysate

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