Ultrafast Screening of a Novel, Moderately Hydrophilic Angiotensin-Converting-Enzyme-Inhibitory Peptide, RYL, from Silkworm Pupa Using an Fe-Doped-Silkworm-Excrement-Derived Biocarbon: Waste Conversion by Waste

Liu, Long; Wei, Yanan; Chang, Qing; Sun, Huaju; Chai, Kungang; Huang, Zuqiang; Zhao, Zhenxia

doi:10.1021/acs.jafc.7b04442

Cited by 26 publications

(15 citation statements)

References 44 publications

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“…Some of them were found to exert two or more activities. Thus, α s1 -CN-derived peptides RY, RYL, RYLG, YLGY and FYPEL exert both ACE-inhibitory and antioxidant activities [ 23 , 24 , 25 , 26 , 27 ]. ACE-inhibitory and opioid activities are exerted by sequences YGFLP [ 28 ] and YGFL [ 29 , 30 ].…”

Section: Resultsmentioning

confidence: 99%

In Silico and In Vitro Analysis of Multifunctionality of Animal Food-Derived Peptides

Amigo

Martínez-Maqueda

Hernández-Ledesma

2020

Foods

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Currently, the associations between oxidative stress, inflammation, hypertension, and metabolic disturbances and non-communicable diseases are very well known. Since these risk factors show a preventable character, the searching of food peptides acting against them has become a promising strategy for the design and development of new multifunctional foods or nutraceuticals. In the present study, an integrated approach combining an in silico study and in vitro assays was used to confirm the multifunctionality of milk and meat protein-derived peptides that were similar to or shared amino acids with previously described opioid peptides. By the in silico analysis, 15 of the 27 assayed peptides were found to exert two or more activities, with Angiotensin-converting enzyme (ACE) inhibitory, antioxidant, and opioid being the most commonly found. The in vitro study confirmed ACE-inhibitory and antioxidant activities in 15 and 26 of the 27 synthetic peptides, respectively. Four fragments, RYLGYLE, YLGYLE, YFYPEL, and YPWT, also demonstrated the ability to protect Caco-2 and macrophages RAW264.7 cells from the oxidative damage caused by chemicals. The multifunctionality of these peptides makes them promising agents against oxidative stress-associated diseases.

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Section: Resultsmentioning

confidence: 99%

In Silico and In Vitro Analysis of Multifunctionality of Animal Food-Derived Peptides

Amigo

Martínez-Maqueda

Hernández-Ledesma

2020

Foods

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“…Competitive inhibitors can compete with the substrate for the catalytic site of the enzyme or can alter the conformation of the enzyme, ultimately inhibiting its activity [ 43 ]. In recent years, many competitive ACE inhibitory peptides have been reported, such as YQK (Tyr-Gln-Lys) from bovine casein [ 44 ], RYL (Arg-Tyr-Leu) from Silkworm Pupa [ 45 ], VVSLSIPR (Val-Val-Ser-Leu-Ser-Ile-Pro-Arg) from pigeon pea ( Cajanus cajan ) [ 46 ], and YLYELAR (Tyr-Leu-Tyr-Glu-Leu-Ala-Arg), AFPYYGHHLG (Ala-Phe-Pro-Tyr-Tyr-Gly-His-His-Leu-Gly) from scorpion ( Hemiscorpius lepturus ) venom. In addition, commercial functional foods or dietary supplements [ 16 , 17 ], as well as many antihypertensive drugs [ 47 ], have also been reported to be competitive inhibitors of ACE.…”

Section: Resultsmentioning

confidence: 99%

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

Zhang

Luo

et al. 2018

Marine Drugs

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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.

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“…Authors used docking to study the mode of action of both peptides. In other work, Liu et al [24] found a hydrophilic peptide (RYL) derived from agricultural waste (silkworm excrement and pupa) with high ACE-inhibitory activity. Authors used docking to study interactions between RYL and its target.…”

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

confidence: 98%

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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Ultrafast Screening of a Novel, Moderately Hydrophilic Angiotensin-Converting-Enzyme-Inhibitory Peptide, RYL, from Silkworm Pupa Using an Fe-Doped-Silkworm-Excrement-Derived Biocarbon: Waste Conversion by Waste

Cited by 26 publications

References 44 publications

In Silico and In Vitro Analysis of Multifunctionality of Animal Food-Derived Peptides

In Silico and In Vitro Analysis of Multifunctionality of Animal Food-Derived Peptides

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

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

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