MICROPOROUS AND MESOPOROUS MATERIALS
·
2023
·
IF 5.2
Zefen Wang,Siyuan Liu,Qian Zhou,Pengru Liu,Dankui Liao,Ping Lan,Bo Peng,Xiongdiao Lan
Immobilized angiotensin converting enzyme (ACE) utilizes specific interaction between ACE and ACE inhibitors to screen drugs for hypertension therapy, but traditional immobilized ACE is insufficient to achieve satisfactory effect for the poor immobilization efficiency and stability. In this work, mesoporous ZIF-8 (mZIF-8) coated with polydopamine (PDA) was developed as an enzyme-immobilization platform for the first time. Molecular docking was used to study the mechanism of ACE induced mZIF-8 synthesis. The immobilized enzyme ACE@mZIF-8/PDA were shown to possess mesoporous structures with ACE encapsulation efficiency of ∼90%. Compared with the free enzyme, ACE@mZIF-8/PDA exhibited enhanced tolerance to temperature, pH, unfolding and proteolytic agents, with excellent reusability (maintained 82.29% ± 4.11% of initial activity after being reused 10 times) and storage stability (retaining 93.12% ± 3.271% residual activity after 30 days). Molecular docking research conformed ACE induced the triggered nucleation of MOFs via binding with MOFs precursors. Moreover, ACE@mZIF-8/PDA was used as high-performance adsorbent for enrichment of ACE inhibitory peptides. The noncompetitive inhibitory peptide GF-6 and competitive inhibitory peptide VPP could be captured synchronously, which avoided the loss of active substances. These results indicated that the ACE@mZIF-8/PDA provides an evolutionary platform for rapid screening of inhibitory peptides.
研究领域:
生物化学
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材料科学
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药物开发
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DOI
高影响因子
Marine Drugs
·
2024
·Vol. 22
·期 7
·305
·
IF 4.9
Wen-Jie Cao,Rui Liu,Wen-Xiao Zhao,Jian Li,Yan Wang,Xiao-Jie Yuan,Hui-Lin Wang,Yu-Zhong Zhang,Xiu-Lan Chen,Yu-Qiang Zhang
Marine bacterial proteases have rarely been used to produce bioactive peptides, although many have been reported. This study aims to evaluate the potential of the marine bacterial metalloprotease A69 from recombinantBacillus subtilisin the preparation of peanut peptides (PPs) with antioxidant activity and angiotensin-converting enzyme (ACE)-inhibitory activity. Based on the optimization of the hydrolysis parameters of protease A69, a process for PPs preparation was set up in which the peanut protein was hydrolyzed by A69 at 3000 U g−1and 60 °C, pH 7.0 for 4 h. The prepared PPs exhibited a high content of peptides with molecular weights lower than 1000 Da (>80%) and 3000 Da (>95%) and contained 17 kinds of amino acids. Moreover, the PPs displayed elevated scavenging of hydroxyl radical and 1,1-diphenyl-2-picryl-hydrazyl radical, with IC50values of 1.50 mg mL−1and 1.66 mg mL−1, respectively, indicating the good antioxidant activity of the PPs. The PPs also showed remarkable ACE-inhibitory activity, with an IC50value of 0.71 mg mL−1. By liquid chromatography mass spectrometry analysis, the sequences of 19 ACE inhibitory peptides and 15 antioxidant peptides were identified from the PPs. These results indicate that the prepared PPs have a good nutritional value, as well as good antioxidant and antihypertensive effects, and that the marine bacterial metalloprotease A69 has promising potential in relation to the preparation of bioactive peptides from peanut protein.
研究领域:
食品科学
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生物化学
·
海洋生物学
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DOI
PubMed
高影响因子
PROCESS BIOCHEMISTRY
·
2023
·
IF 4.4
Qi Liu,Shan Shao,Jingyu Bao,Syed Jalil Shah,Shumin Yue,Xinqi Luan,Qing Liu,Linguang Xing,Zhongfeng Shi,Zhenxia Zhao,Zhongxing Zhao
The 3D-QSAR model is one of the most effective techniques for predicting the peptide bioactivity based on their structure properties. The accuracy of model prediction is highly dependent on the bio-activity of the peptides in its dataset. However, the same peptide used for constructing the database was reported to have obviously different activities in different published articles, which may significantly decrease the prediction accuracy. Based on this, we chose ACE inhibitory (ACE-I) dipeptides that can be absorbed directly into the human small intestine as research object. Ten dipeptides were randomly selected from the literatures for molecular docking with ACE and synthesized to test their activity. Ultimately, a linear equation was developed between bio-activities and docking scores, which was used to revalidate the reliable ACE-I activities of all reported dipeptides for constructing a credible dataset of 3D-QSAR model. The prediction accuracy was significantly enhanced and the model we established had a high Q 2 = 0.840 and R 2 = 0.998. Furthermore, dipeptide CW was predicted and tested in vitro to achieve the highest ACE-I activity (IC 50 = 0.16 μM), and the inhibition mechanism was also investigated. This study introduced a new method for predicting bio-activity with high precision using the 3D-QSAR model.
研究领域:
生物信息学
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药物化学
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生物化学
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DOI
高影响因子
Food Bioscience
·
2023
·
IF 5.2
Zhengli Lin,Hui Wu,Mengmeng Zhang
Earthworms are a good protein resources with several health-promoting effects, particularly for antihypertensive activity. However, the active components remain unknown. In the present study, earthworms’ protein in vitro gastrointestinal digestion product (EWP-GI) was prepared and purified by ultrafiltration and column chromatography. The potential angiotensin-converting enzyme (ACE) inhibitory peptides were identified using UPLC-MS/MS and screened using in silico tools and molecular docking. Finally, seven novel ACEI peptides (SSPLWER, RFFGP, LERWP, MFPGIADR, FPGIADR, SADRISHGF and ADRYSSWP) were obtained. The two most active peptides, SSPLWER and RFFGP, presented ACE inhibitory activity with IC 50 values of 14.30 ± 0.81 and 117.63 ± 0.36 μM respectively, and both acted as competitive inhibitors. The peptides occupied the active sites of ACE to generate steric hindrance, which weakened the catalytic reaction. Moreover, the tryptophan residue in SSPLWER and the arginine residue in RFFGP played an important role in the ACE inhibitory effects of peptides. Thus, these results indicated that peptides were the active ingredients of earthworms that exerted ACE inhibitory activity after gastrointestinal digestion, offering a new perspective to further enlighten the hypotensive activity of earthworm.
研究领域:
生物化学
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药理学
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食品科学
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产品关联
DOI
高影响因子
JOURNAL OF ECONOMIC ENTOMOLOGY
·
2025
·
IF 2.4
Cao Li-Xia,Pan Xing-Run,Zhang Wan-Na,Lu Jing-Bo,Hu Zhi-Kang,Sheng Cheng-Wang,Peng Ying-Chuan
The fall armyworm (Spodoptera frugiperda), a lepidopteran pest of highly destructive, has developed resistance to organophosphate and carbamate insecticides through target-site mutations, including A201S and F290V in the ace-1 gene encoding acetylcholinesterase (AChE). Developing rapid and reliable methods to detect these mutations is crucial for monitoring resistance and guiding effective management strategies. Although S. frugiperda populations remain sensitive to the tested insecticides, the A201S and F290V mutations were identified in collected field samples. To facilitate detection, a sensitive and field-deployable loop-mediated isothermal amplification (LAMP) assay was developed, targeting these mutations within the ace-1 gene of S. frugiperda. The specificity and sensitivity of the LAMP assay was optimized for rapid detection, with reactions performed at 68 °C for 80 min. Results were visualized through color change and confirmed by gel electrophoresis. Validation using DNA from laboratory and field samples demonstrated complete agreement between the LAMP assay and DNA sequencing, affirming the accuracy and reliability of the method. The developed LAMP assay provides a simple, rapid, and effective tool for detecting the A201S and F290V mutations in the ace-1 gene of S. frugiperda. The assay’s simplicity, isothermal operation, and clear visual results make it a valuable tool for resistance monitoring and integrated pest management in agricultural settings.
研究领域:
昆虫学
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分子生物学
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农药学
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农业害虫管理
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DOI
PubMed
高影响因子
JOURNAL OF FOOD BIOCHEMISTRY
·
2021
·Vol. 45
·期 4
·e13638
·
IF 2.72
Xin Lu,Qiang Sun,Lixia Zhang,Ruidan Wang,Jinhong Gao,Cong Jia,Jinian Huang
To prepare and identify ACE-inhibitory peptides originated from sesame seed protein, peptides with strong ACE-inhibitory activities were obtained via the optimization of protease and hydrolysis conditions, and these peptides were purified and identified by membrane separation, gel filtration, and liquid chromatography–mass spectrometry. Results showed that the dual-enzyme comprised alcalase and trypsin with the enzyme activity ratio of 3:7 was suitable to produce ACE-inhibitory peptides. The highest ACE-inhibitory activity of 98.10 ± 0.26% was obtained at the following parameters, pH 8.35, E/S ratio of 6,145 U/g, and hydrolysis time of 4.4 hr. ISGAQPSLR and VVISAPSK ranked the first and second ACE-inhibitory activity among 15 identified ACE-inhibitory peptides. Both peptides influenced ACE via binding with the S1 pocket, S2 pocket, and Zn 2+ ion. ISGAQPSLR even impacted the S1′ pocket. ISGAQPSLR and VVISAPSK acted as a competitive and noncompetitive inhibitor, respectively. ACE-inhibitory peptides derivated from sesame seed protein have potential applications in functional food. Practical applications Although sesame seed protein is proven as the precursor of ACE-inhibitory peptide, preparing ACE-inhibitory peptide from sesame seed protein is still suffering from insufficient information on hydrolysis condition and the peptide sequence. Therefore, the performance of the typical protease on preparing ACE-inhibitory peptide from sesame seed protein has been evaluated, the effect of the amino acid composition of sesame seed protein and cleavage specificity of protease on the generation of ACE-inhibitory peptide has been investigated, hydrolysis conditions have been optimized, the peptide sequence has been identified to illuminate the effect of sesame seed protein fraction on the formation of ACE-inhibitory peptide and discuss the structural characteristics. ACE-inhibitory peptides originating from sesame seed protein could apply in functional food. It is promising for dual-enzyme hydrolysis to utilize in preparation of high-value bioactive peptides.
研究领域:
食品科学
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生物化学
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药理学
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产品关联
DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2025
·
IF 6.6
Li Zhang,Qiao Huang,Wan-Ying Gong,Wen-Jing Wang,Chun-Ting Yang,Wei-Tao Zhang,Jun Sheng,Jing Xie,Yang Tian
Walnut protein, a high-quality plant protein, shows potential as a source of ACE inhibitory peptides. Digestive enzymes can effectively hydrolyze walnut protein to release peptide fragments with ACE inhibitory activity. However, existing research has focused on the overall digestive process, with limited exploration into how digestive enzymes hydrolyze walnut protein and the biological characteristics of the hydrolysates, particularly their ACE inhibitory activity. In this study, walnut protein was hydrolyzed using pepsin, trypsin, and chymotrypsin. Our results showed that chymotrypsin efficiently hydrolyzed walnut protein, with the chymotrypsin hydrolysate exhibiting the highest ACE inhibitory activity, demonstrated by an IC 50 value of 1.725 mg/mL. Further analysis revealed that the chymotrypsin hydrolysate was rich in hydrophobic and aromatic amino acids, which correlated positively with ACE inhibition. The highly active peptide YHP was identified through molecular docking and exhibited competitive inhibition properties, with an IC 50 value of 0.248 mg/mL. Molecular dynamics simulations, isothermal titration calorimetry, and atomic force microscopy analyses confirmed the stability and affinity of YHP for binding to ACE. Additionally, YHP demonstrated high stability during simulated gastrointestinal digestion. This study provides a significant foundation for the advanced processing of walnut protein and the development of novel ACE inhibitors.
研究领域:
生物化学
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食品科学
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药理学
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分子生物学
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生物物理学
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营养科学
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酶学
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产品关联
DOI
高影响因子
FOOD RESEARCH INTERNATIONAL
·
2021
·
IF 6.475
Shan Shao,Huaju Sun,Yaseen Muhammad,Hong Huang,Ruimeng Wang,Shuangxi Nie,Meiyun Huang,Ziyi Zhao,Zhongxing Zhao
Efficient screening of angiotensin converting enzyme inhibitory (ACE-I) peptides from agricultural or edible sources attract increasing attention. However, their purification process from the complex natural system is still semi-empirical or even uncontrollable, which has seriously reduced their screening efficiency. Herein, inspired by the prediction of ACE-I activity, 3D-QSAR was proposed to predict the adsorption performance of peptides from sericin hydrolysate (SH) having high ACE-I activity on porous hypercross-linked polymers according to their molecular structures. Thiophene hypercross-linked polymer (T-HCP) possessing better screening capacity for ACE-I peptides was chosen as our research object in this work. The sequence and relative adsorption rate of 101 peptides in SH were analyzed by LC-MS and was used as a database to construct the relationship of peptide’s chemical structure and adsorption performance on T-HCP by Comparative molecular similarity indices analysis (CoMSIA) from 3D-QSAR. Optimum CoMSIA revealed that enhanced interaction of hydrophobicity and H-bond between T-HCP and the peptide was conducive to increase the adsorption performance of di- to hexa- peptides. Based on these relationships, the adsorption capability of 24 designed peptides with distinguished hydrophobic and H-bond fields was predicted on T-HCP by using optimum CoMSIA and the results of half of these were verified, which showed high consistency with their predicted adsorption rate. Interestingly, these peptides having higher adsorption capacities on T-HCP also possessed higher ACE-I activity. This can be attributed to the high concentration of aromatic surface with π-π interaction and weak-polar C S C group with H-bond interaction on T-HCP material, which is ideal for the selective adsorption of peptides with higher ACE-I activity from SH. This study provides important theoretical guidance for the industrial screening of bio-functional peptides from complex protein mixtures.
研究领域:
生物化学
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食品科学
·
药物开发
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DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2024
·
IF 8.5
Jianfei Li,Haohan Hu,Xiya Chen,Haiting Zhu,Wenhao Zhang,Zhiyuan Tai,Xiaodong Yu,Qiyi He
Angiotensin I-converting enzyme (ACE) regulates blood pressure through the renin-angiotensin system. Douchi, a traditional fermented soybean condiment, may have antihypertensive effects, but research on ACE inhibitory peptides from Douchi hydrolysates is limited. We hypothesized that enzymatic treatment could enhance ACE inhibitory peptide diversity and efficacy. We tested ten single enzymes and four combinations, finding pepsin-trypsin-chymotrypsin most effective. Hydrolysates were purified using Sephadex G-15 and reversed-phase HPLC, and peptides were identified via LC-MS/MS. Five peptides (LF, VVF, VGAW, GLFG, NGK) were identified, with VGAW as the most potent ACE inhibitor (IC 50 46.6 ± 5.2 μM) showing excellent thermal and pH stability. Lineweaver-Burk plots confirmed competitive inhibition, and molecular docking revealed eight hydrogen bonds between VGAW and ACE. In hypertensive rats, VGAW significantly reduced blood pressure at 12.5, 25, and 50 mg/kg. These findings highlight Douchi as a source of ACE inhibitory peptides and suggest VGAW as a promising functional food ingredient.
研究领域:
药理学
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食品科学
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生物化学
·
高血压研究
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产品关联
DOI
PubMed
高影响因子
JOURNAL OF APPLIED PHYCOLOGY
·
2022
·Vol. 34
·期 3
·1497-1511
·
IF 3.404
Liu Jing,Bai Xinpeng,Fu Pengcheng
Arthrospira platensis proteins are considered as viable ingredients for functional foods with nutraceutical properties and health-promoting effects. In this study, we used five different proteases including pepsin, trypsin, alcalase, papain, and bromelain to hydrolyze A. platensis phycobiliprotein. LC–MS/MS (liquid chromatography-tandem mass spectrometry) was used to determine the composition of the hydrolysates with thousands of bioactive peptides. Based on peptide sequencing, a candidate list of 1,333 bioactive peptides was constructed for the first time for which bioinformatics tools were used to assess the properties of the bioactive peptides. The inhibitory activity of dipeptidyl peptidase IV (DPP-IV) and angiotensin-converting enzyme (ACE), as well as the antioxidant activity of five phycobiliprotein hydrolysates (PBPHs), were verified in vitro. The IC 50 values of PBPH-pepsin, PBPH-trypsin, PBPH-alcalase, PBPH-papain, and PBPH-bromelain for DPP-IV inhibited activity were determined to be 4.059, 5.603, 5.257, 3.819, and 4.195 mg mL −1 , respectively. All the above five PBPHs were also seen to significantly inhibit ACE activity ( P < 0.0001) in the range of 0.1–1.0 mg mL −1 . The activity of five PBPHs fraction was found for the 2-azino-bis (3-ethylbenzothiazoline6-sulfonic acid) diammonium salt (ABTS) assay (the highest was 1.37 mM Trolox equivalent of 30 mg mL −1 of PBPH-trypsin), 1,1diphenyl-2-picrylhydrazyl (DPPH) assay (the highest was 204.67 µM Trolox equivalent of 10 mg mL −1 of PBPH-pepsin), and Fe 2+ chelating ability (the highest was 639.73 µM FeSO 4 equivalent of 10 mg mL −1 of PBPH-trypsin). This study indicated that it was feasible to utilize A. platensis phycobiliprotein as a source of bioactive peptides which may be used as functional food and/or nutritional supplements for human health.
研究领域:
食品科学
·
生物化学
·
营养学
·
药理学
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产品关联
DOI
高影响因子
PROCESS BIOCHEMISTRY
·
2020
·
IF 2.952
Kai Lin,Zhao Ma,Mythili Ramachandran,Cristabelle De Souza,Xue Han,Lan-wei Zhang
The purpose of this study was to explore the effects of KYIPIQ, an angiotensin I-converting enzyme (ACE) inhibitory peptide found in yak milk casein, on the production of nitric oxide (NO) in human vascular endothelial cells (HUVECs). Additionally, we also sought to study the transport pathway of this peptide across monolayers of the human epithelial colorectal adenocarcinoma cell line (Caco-2). Treatment with peptide KYIPIQ increased NO synthesis and expression of phosphorylated endothelial nitric oxide synthase (eNOS) in HUVECs. Our results demonstrate that KYIPIQ-induced eNOS phosphorylation is dependent on the protein kinase B (Akt) activation pathway. Furthermore, our data indicate that the peptide KYIPIQ can be transported across the Caco-2 cell monolayer and that paracellular transport is the main transcellular mechanism. Thus, our studies suggest that KYIPIQ can be potentially used as a therapeutic agent for the treatment of hypertension.
研究领域:
药理学
·
细胞生物学
·
分子生物学
·
心血管科学
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产品关联
DOI
高影响因子
FOOD CHEMISTRY
·
2024
·
IF 8.5
Haotong Zhang,Li Liang,Baoguo Sun,Rui Yang,Zunying Liu,Xiangzhao Mao,Yuyu Zhang
Angiotensin-I-converting enzyme (ACE) inhibitory activity and saltiness-enhancing properties of chicken-derived umami peptides were investigated. DGGRYY and NEFGYSNR were screened and the IC 50 values were 28.71 μM and 283.24 μM, indicating their potential as novel ACE inhibitors. DGGRYY and NEFGYSNR have good pH and thermal stability. After gastrointestinal digestion, the ACE-inhibitory activity of DGGRYY retained about 53 %, whereas NEFGYSNR retained about 57 %. The inhibition pattern of both peptides was determined to be uncompetitive, consisting with the result of multiple ligand docking that the binding sites were outside the ACE active pocket. Trp59, Tyr62, Asp121, Arg124, and Ser516 were the key binding sites that contributed to the total binding energy. In addition, saltiness and palatability models were established according to sensory analysis and central composite design. In 0.1 % ∼ 0.3 % NaCl solutions, the addition of DGGRYY and NEFGYSNR could enhance the salty intensity and compensate for the palatability loss caused by salt reduction.
研究领域:
食品科学
·
生物化学
·
营养学
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产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）