Quantitative Structure–Activity Relationship Modeling Coupled with Molecular Docking Analysis in Screening of Angiotensin I-Converting Enzyme Inhibitory Peptides from Qula Casein Hydrolysates Obtained by Two-Enzyme Combination Hydrolysis

Lin, Kai; Zhang, Lanwei; Han, Xue; Zhang, Meng; Zhang, Jianming; Wu, Yifan; Cheng, Dansong

doi:10.1021/acs.jafc.8b00313

Cited by 52 publications

(37 citation statements)

References 43 publications

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“…Bioactive peptides encrypted within the natural food protein are supposed to be released by enzymolysis to exert their biological function. A number of food processing enzymes were previously used for the generation of bioactive peptides from a variety of natural sources (Fu, Wu, Zhu, & Xiao, ; Lin, Zhang, Han, Meng, et al, ). In our study, three commercial plant proteases papain, ficin, and stem bromelain were applied, respectively, to the selected quinoa protein sequences by “Enzyme(s) action” of BIOPEP (Appendix S2).…”

Section: Resultsmentioning

confidence: 99%

“…BIOPEP database, providing collection of sequences (proteins, bioactive peptides, allergenic proteins, and sensory peptides), can be used to predict biological activities about a protein sequence, and to estimate the release of bioactive peptides by proteolysis simulation using certain proteases (Minkiewicz, Dziuba, Iwaniak, Dziuba, & Darewicz, ). This in silico tools has been successfully applied in the investigation of bioactive peptides from different sources, including animal products, plant products, and seafood products, such as bovine meat proteins (Minkiewicz, Dziuba, & Michalska, ), porcine myofibrillar proteins (Kęska & Stadnik, ), yak milk casein (Lin et al, ), cereal storage proteins (Cavazos & de Mejia, ), oilseed proteins (Han, Maycock, Murray, & Boesch, ), giant grouper roe proteins (Panjaitan, Gomez, & Chang, ), and portuguese oyster proteins (Gomez, Peralta, Tejano, & Chang, ). In addition, online tool PeptideRanker has the function of predicting the potential bioactive index of peptides, and ToxinPred has been developed to predict the toxicity of peptides.…”

Section: Introductionmentioning

confidence: 99%

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Novel dipeptidyl peptidase‐IV and angiotensin‐I‐converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis

Guo

Richel

Hao

et al. 2020

Food Science & Nutrition

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Quinoa protein has been paid more and more attention because of its nutritional properties and beneficial effects. With the development of bioinformatics, bioactive peptide database and computer‐assisted simulation provide an efficient and time‐saving method for the theoretical estimation of potential bioactivities of protein. Therefore, the potential of quinoa protein sequences for releasing bioactive peptides was evaluated using the BIOPEP database, which revealed that quinoa protein, especially globulin, is a potential source of peptides with dipeptidyl peptidase‐IV (DPP‐IV) and angiotensin‐I‐converting enzyme (ACE) inhibitory activities. Three plant proteases, namely papain, ficin, and stem bromelain, were employed for the in silico proteolysis of quinoa protein. Furthermore, four tripeptides (MAF, NMF, HPF, and MCG) were screened as novel promising bioactive peptides by PeptideRanker. The bioactivities of selected peptides were confirmed using chemical synthesis and in vitro assay. The present work suggests that quinoa protein can serve as a good source of bioactive peptides, and in silico approach can provide theoretical assistance for investigation and production of functional peptides.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Novel dipeptidyl peptidase‐IV and angiotensin‐I‐converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis

Guo

Richel

Hao

et al. 2020

Food Science & Nutrition

View full text Add to dashboard Cite

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“…Finally, they explored their interaction mechanisms and bonding configurations with ACE by using docking and molecular dynamics (MD) simulations. In other interesting report, Lin et al [32] hydrolyzed Qula casein derived from yak milk casein and screened high ACE inhibitory activity peptides by using quantitative structure-activity relationship (QSAR) modeling integrated with molecular docking analysis. On the basis of the QSAR modeling predictions, authors selected a total of 16 peptides for molecular docking analysis and their docking study revealed that four of the peptides (KFPQY, MPFPKYP, MFPPQ, and QWQVL) bound the active site of 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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“…From the perspective of cheese processing, milk with such high levels of dry matter is well suited for cheese making. Every year, more than 1.6 million tonnes of yak milk are produced in the southwest region of China, including the Qinghai, Gansu, Sichuan, and Tibet areas (Lin et al, 2018). However, little of the milk was processed into cheese due to the diet habits of local people, and the cheese making properties of yak milk have seldom been reported.…”

Section: Introductionmentioning

confidence: 99%

Composition, coagulation characteristics, and cheese making capacity of yak milk

Zhang

Yang

Cai

et al. 2020

Journal of Dairy Science

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Yak is one of the few species of which the rennetcoagulated cheese making characteristics of its milk are still not well understood. This study investigated composition and rennet-induced coagulation properties of milk from 17 individual yak cows in comparison with milk from 32 individual Holstein cows. Yak cows produced milk with generally higher concentrations of milk components. The concentrations of fat, protein, solids-not-fat (SNF), and calcium in yak milk were 1.89-, 1.68-, 1.46-, and 2-fold those in Holstein milk, respectively. The hydrodynamic radii of casein micelles (187.25 nm) and chymosin-induced paracasein (1,620 nm) were about twice the sizes of those found in Holstein milk. Higher concentrations of calcium in yak milk, together with larger sizes of casein micelles, explains the reason for its fast rate of curd formation and firmer curd texture. Optical microrheology analysis also showed that Ca 2+ concentration had greater influence on the coagulation of yak milk than on Holstein milk. Cheese making trials with yak and Holstein milk proved the higher cheese yield of yak milk: 1.67-fold that of Holstein milk. Therefore, yak milk could be a suitable source of milk for enzyme-coagulated cheese making.

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Quantitative Structure–Activity Relationship Modeling Coupled with Molecular Docking Analysis in Screening of Angiotensin I-Converting Enzyme Inhibitory Peptides from Qula Casein Hydrolysates Obtained by Two-Enzyme Combination Hydrolysis

Cited by 52 publications

References 43 publications

Novel dipeptidyl peptidase‐IV and angiotensin‐I‐converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis

Novel dipeptidyl peptidase‐IV and angiotensin‐I‐converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

Composition, coagulation characteristics, and cheese making capacity of yak milk

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