文献检索

查找使用阿拉丁产品的科研文献

检索与阿拉丁产品相关的同行评审论文、DOI、PubMed 编号、期刊、作者、CAS 号及研究领域。

科研影响力快照

与阿拉丁产品相关的已发表科研成果

在搜索之前,这些指标可帮助访客快速了解产品关联科研的规模与质量。

346,364+ SCI 论文 与阿拉丁产品引用相关
2,295,288.15 总影响因子 匹配文献记录中影响因子的总和
81.20 最高期刊影响因子 匹配期刊中的最高 IF
6.63 平均期刊影响因子 匹配文献的平均 IF

参考指标 指标基于阿拉丁文献引用数据库及期刊影响因子记录。文献关联仅供科研参考,请以原始文献为准。

热门产品

视图 列表 网格

显示第1至12个,产品总数17个

设置提升方向
ACE抑制肽
Biomolecules · 2024 ·Vol. 14 ·期 5 ·581 · IF 4.8

Novel Angiotensin-Converting Enzyme-Inhibitory Peptides Obtained from Trichiurus lepturus: Preparation, Identification and Potential Antihypertensive Mechanism

Jiaming Cao,Boyuan Xiang,Baojie Dou,Jingfei Hu,Lei Zhang,Xinxin Kang,Mingsheng Lyu,Shujun Wang

Peptides possessing antihypertensive attributes via inhibiting the angiotensin-converting enzyme (ACE) were derived through the enzymatic degradation ofTrichiurus lepturus(ribbonfish) using alkaline protease. The resulting mixture underwent filtration using centrifugation, ultrafiltration tubes, and Sephadex G-25 gels. Peptides exhibiting ACE-inhibitory properties and DPPH free-radical-scavenging abilities were isolated and subsequently purified via LC/MS-MS, leading to the identification of over 100 peptide components. In silico screening yielded five ACE inhibitory peptides: FAGDDAPR, QGPIGPR, IFPRNPP, AGFAGDDAPR, and GPTGPAGPR. Among these, IFPRNPP and AGFAGDDAPR were found to be allergenic, while FAGDDAPRR, QGPIGPR, and GPTGPAGP showed good ACE-inhibitory effects. IC50values for the latter peptides were obtained from HUVEC cells: FAGDDAPRR (IC50= 262.98 μM), QGPIGPR (IC50= 81.09 μM), and GPTGPAGP (IC50= 168.11 μM). Peptide constituents derived from ribbonfish proteins effectively modulated ACE activity, thus underscoring their therapeutic potential. Molecular docking and modeling corroborated these findings, emphasizing the utility of functional foods as a promising avenue for the treatment and prevention of hypertension, with potential ancillary health benefits and applications as substitutes for synthetic drugs.

研究领域: 食品科学 · 生物化学 · 药理学
✓ 已验证 产品关联 DOI PubMed 高影响因子
查看原文 查看 PubMed
Food & Function · 2018 ·Vol. 9 ·期 4 ·2270-2281 · IF 3.289

Whole-grain oats (Avena sativa L.) as a carrier of lactic acid bacteria and a supplement rich in angiotensin I-converting enzyme inhibitory peptides through solid-state fermentation

Han Wu,Xin Rui,Wei Li,Yu Xiao,Jianzhong Zhou,Mingsheng Dong

This study explored a novel strategy to develop solid-state whole-grain oats as a novel carrier of lactic acid bacteria and a nutraceutical supplement rich in ACE inhibitory peptides. Oats were fermented by Lactobacillus plantarum B1-6, Rhizopus oryzae, or a combination of L. plantarum B1-6 and R. oryzae. L. plantarum showed a much better growth performance in oats when it was combined with R. oryzae than when it was cultured alone, as evidenced by an increase in viable cell count to 9.70 log cfu g−1 after 72 h of fermentation. The coinoculated fermented oats (CFO) and the R. oryzae-fermented oats (RFO) were then selected for investigations on protein hydrolysis and on the functional properties of the released bioactive peptides. The results showed that the soluble protein contents changed from 7.05 mg g−1 to 14.43 and 10.21 mg g−1 for CFO and RFO, respectively. However, the degree of hydrolysis and the content of peptides with molecular masses less than 10 000 Da indicated that the CFO proteins can be degraded to a greater degree. As analyzed by electrophoresis and reversed-phase high-performance liquid chromatography, the protein and peptide profiles of CFO and RFO demonstrated that the proteins from CFO were more obviously hydrolyzed and more small peptides were obtained. In addition, both CFO and RFO presented higher ACE inhibitory activities than unfermented oats, whereas the protein extracts from CFO exerted a lower IC50 value of 0.42 mg protein per mL compared with the protein extracts from the other samples. This research has broadened our knowledge on the development of whole-grain oat products as a probiotic carrier and on the difference between mixed solid-state fermentation (SSF) and fungi SSF in terms of protein degradation and the capacity to release ACE inhibitory peptides. Our approach could be used to obtain probiotic food products and probably to develop oats as a potential therapeutic ingredient targeting hypertension.

CAS / MDL: 76-05-1 7681-93-8
研究领域: 食品科学 · 微生物学 · 营养学
✓ 已验证 产品关联 DOI PubMed 高影响因子
查看原文 查看 PubMed
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2017 · IF 3.154

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

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

A novel, moderately hydrophilic peptide (RYL) with high ACE-inhibitory activity was screened ultrafast via a concept of waste conversion using waste. This novel peptide was screened from silkworm pupa using an Fe-doped porous biocarbon (FL/Z-SE) derived from silkworm excrement. FL/Z-SE possessed magnetic properties and specific selection for peptides due to Fe’s dual functions. The selected RYL, which has moderate hydrophilicity (LogP = −0.22), exhibited a comparatively high ACE-inhibitory activity (IC50 = 3.31 ± 0.11 μM). The inhibitory kinetics and docking-simulation results show that, as a competitive ACE inhibitor, RYL formed five hydrogen bonds with the ACE residues in the S1 and S2 pockets. In this work, both the screening carbon material and the selected ACE-inhibitory peptide were derived from agricultural waste (silkworm excrement and pupa), which offers a new way of thinking about the development of advanced uses of the silkworm byproducts and wastes.

CAS / MDL: 7646-85-7 7758-94-3
研究领域: 生物技术 · 环境科学 · 药学
✓ 已验证 产品关联 DOI PubMed 高影响因子
查看原文 查看 PubMed
Food Bioscience · 2025 · IF 5.9

Novel angiotensin-I-converting enzyme (ACE) inhibitory peptides from Porphyra haitanensis: Screening, digestion stability, and mechanistic insights

Xianjiang Ye,Ran Yang,Zhizhi Yang,Baote Huang,Talha Riaz,Chao Zhao,Jicheng Chen

Food-derived peptides with angiotensin-I-converting enzyme inhibitory (ACEI) activity have garnered significant research attention. This study focused on examining ACEI peptides from Porphyra haitanensis and investigating their potential inhibitory mechanisms through a combination of in silico and in vitro methods. Five novel potential ACEI peptides (ASF: Ala-Ser-Phe, EIIL: Glu-Ile-Ile-Leu, LCVPR: Leu-Cys-Val-Pro-Arg, LDVVN: Leu-Asp-Val-Val-Asn, and LSPSW: Leu-Ser-Pro-Ser-Trp) were identified through a combination of peptidomics and in silico bioinformatics analysis, of which LSPSW showed the highest activity (IC 50 : 5.27 ± 0.53 μM). After simulated gastrointestinal digestion (SGD), the activities of LCVPR and LSPSW remained almost unchanged. The results from inhibition kinetics and molecular docking demonstrated that ACEI peptides with differing inhibition mechanisms could successfully bind to ACE through hydrogen bonds. Based on network pharmacology analysis and cellular experiments, LSPSW exerted antihypertensive effects by regulating the expression levels of peroxisome proliferator activated receptor gamma (PPARG), prostaglandin-endoperoxide synthase 2 (PTGS2), and renin (REN). This research provided a novel theoretical foundation for the high-value application of P. haitanensis .

研究领域: 食品科学 · 生物信息学 · 药理学
✓ 已验证 产品关联 DOI 高影响因子
查看原文 查看 PubMed
LWT-FOOD SCIENCE AND TECHNOLOGY · 2021 · IF 4.952

Efficient enzymatic production of angiotensin I-converting enzyme inhibitory peptides from three protein-rich materials by electrolyzed water pretreatment

Peng Zhang,Chang Chang,Haijie Liu,Qiaojuan Yan,Zhengqiang Jiang

Three protein-rich materials were pretreated with a self-designed alkaline electrolyzed water (AEW) pretreatment equipment to promote the release of angiotensin I-converting enzyme (ACE) inhibitory peptides by improving hydrolysis efficiency. According to degree of hydrolysis (DH) and ACE inhibitory activity, defatted walnut meal (DWM) was selected to study antihypertensive activity by hydrolysis in assistance of AEW pretreatment. It was found DWM pretreated with AEW at pH 11.5 followed by Alcalase hydrolysis exhibited the highest DH (21.96%), protein recovery rate (94.76%), and ACE inhibitory activity (IC 50 of 0.137 mg/mL), in which AEW pretreatment resulted in the transformation of α-helix and β-turn to random coil and the destruction of hydrogen bonds to expose more cleavage sites to enhance hydrolysis efficiency. Thereafter, ACE inhibitory peptides GIENYRVV (IC 50 of 0.102 mg/mL) and AGRISTVNSHTLPVL (IC 50 of 0.20 mg/mL) were identified from the hydrolysate. Overall, AEW pretreatment was an innovative strategy to promote the release of antihypertensive peptides during hydrolysis.

CAS / MDL: 7758-02-3
研究领域: 食品科学 · 生物化学
✓ 已验证 产品关联 DOI 高影响因子
查看原文 查看 PubMed
INTERNATIONAL DAIRY JOURNAL · 2025 · IF 3.4

Exploration and molecular mechanism of novel ACE inhibitory peptides from goat milk protein: A combined in silico and in vitro study

Ruikai Zhu,Hong Zhang,Yulong Wu,Huanhuan Li,Honggang Tang,Xianrong Xu,Ke Zhao

Hypertension poses a significant threat to human health, and the efficient exploration of food-derived ACEI peptides as milder and safer alternatives to ACEI drugs has garnered increasing attention. Therefore, a combined in silico and in vitro study was performed to investigate novel ACEI peptides from goat milk proteins. First, the papain plus proteinase K was identified as the best enzymatic combination for generating ACEI peptides using BIOPEP. Then the enzymatic conditions of the papain/proteinase, the input order of the enzymes, and the molecular weight (MW) of the hydrolysate were further optimized to obtain the hydrolysate with the highest ACEI activity. Under the optimized condition described, 698 peptides (<25 AA) were successfully identified from the milk hydrolysate of goat (MW < 3 KDa). Among them, six potential novel ACEI peptides were efficiently screened virtually. Verification studies using synthesized peptides partially confirmed the in silico results, with four out of the six selected peptides (FKF, FRY, RWL, and WKP) exhibiting ACEI activity. Additionally, the blood pressure-lowering effects of the top two ACEI peptides (FRY and FKF) were further validated in spontaneously hypertensive rats (SHRs), and FRY treatment significantly lowered the blood pressure of SHRs. To summarize, this study established a rapid enzymatic hydrolysis system for screening novel ACEI peptides and identified a novel antihypertensive peptide, FRY, which provides a new method for research on bioactive peptides research and high-value utilization of goat milk.

CAS / MDL: 39450-01-6 9001-73-4
研究领域: 食品科学 · 分子生物学 · 医学
✓ 已验证 产品关联 DOI 高影响因子
查看原文 查看 PubMed
Foods · 2019 ·Vol. 8 ·期 9 ·390 · IF 3.011

In Vitro Production and Identification of Angiotensin Converting Enzyme (ACE) Inhibitory Peptides Derived from Distilled Spent Grain Prolamin Isolate

Dong Wei,Wenlai Fan,Yan Xu

Distilled spent grain (DSG), the biggest by-product of the Chinese liquor industry, is rich in protein (167.8 g/kg DSG dry weight (DW)). Accounting for 60% of the total protein, prolamins are isolated from dried DSG (DDSG). In this study, angiotensin-converting enzyme (ACE) inhibitory peptides were screened from the prolamin hydrolysates of DDSG using two independent active-directed separations, ultrafiltration and reversed phase high performance liquid chromatography (RP-HPLC) coupled with ACE inhibitory activity evaluation. Six novel ACE inhibitory peptides, AVQ, YPQ, NQL, AYLQ, VLPVLS, and VLPSLN, were successfully identified and quantified from the active RP-HPLC fractions. AVQ and YPQ exhibited the highest activity, having the concentration inducing 50% inhibition (IC50) values for ACE of 181.0 and 220.0 μM, respectively. It was observed that VLPVLS was the most abundant peptide (16.96 mg/g DW) in prolamins. The results indicated that prolamin hydrolysates from DDSG could be served as a source of ACE inhibitory peptides.Keywords:distilled spent grain (DSG);baijiu (Chinese liquor);ACE inhibitory peptides;Prolamin isolate hydrolysates;RP-HPLC;AVQ;YPQ

CAS / MDL: 3483-12-3 643-79-8
研究领域: 食品科学 · 生物化学 · 药学
✓ 已验证 产品关联 DOI PubMed 高影响因子
查看原文 查看 PubMed
Molecular Informatics · 2017 ·Vol. 36 ·期 9 ·1600157 · IF 1.955

Studies on the Bioactivities of ACE-inhibitory Peptides with Phenylalanine C-terminus Using 3D-QSAR, Molecular Docking and in vitro Evaluation

Chunyan Qi,Guimei Lin,Rong Zhang,Wenjuan Wu

Graphical 3D-QSAR, molecular docking and activity evaluation were used to study the bioactivities of ACE-inhibitory peptides with phenylalanine C-terminus. Both CoMFA ( Q 2 =0.773, R 2 =0.992) and CoMSIA ( Q 2 =0.664, R 2 =0.990) models were constructed. According to the established models, four novel potent ACE-inhibitory tripeptides GEF, VEF, VRF, and VKF were synthesized. The IC 50 values were respectively determined to be 13 μM, 23 μM, 5 μM, and 11 μM by in vitro evaluation. The results show good agreement with the predicted values. The established models play an important role in revealing the structure-activity relationship of ACE-inhibitory peptides and designing novel peptides with enhanced biological activity.

CAS / MDL: 495-69-2
研究领域: 药理学 · 生物化学 · 计算化学
✓ 已验证 产品关联 DOI PubMed 高影响因子
查看原文 查看 PubMed
EUROPEAN FOOD RESEARCH AND TECHNOLOGY · 2020 ·Vol. 246 ·期 7 ·1483-1494 · IF 2.366

Preparation, physicochemical characterization and identification of two novel mixed ACE-inhibiting peptides from two distinct tea alkali-soluble protein

Zhu Jiangxiong,Du Mengke,Wu Meirong,Yue Pengxiang,Yang Xiufang,Wei Xinlin,Wang Yuanfeng

In this study, two novel mixed ACE-inhibiting peptides, namely Se-TAPep 1 and TAPep 1, were prepared and purified from selenium-enriched and common alkali-soluble proteins using a series of process, and then its physicochemical properties and oligopeptide sequence were analyzed. The results showed that Se-TAPep 1 and TAPep 1 could be successfully separated, but their ACE inhibitory activities were different (IC50 values were 13.39 mg/mL and 23.56 mg/mL, respectively), this may be related to the difference in selenium content. Further analysis of physicochemical properties showed that the protein or peptide fractions contained their characteristic absorption peaks and contained aromatic amino acids, while the apparent morphology was different, the presence of selenium could change the apparent morphology of protein or polypeptide fractions, arranging of selenium-enriched fractions more irregular. The amino acid composition analysis showed that the Pro content of the selenium-enriched fractions was higher than that of the ordinary component, whereas the oligopeptide sequence analysis showed that both LQPSLGFP derived from Se-TAPep 1 and AETGEIKGHY derived from TAPep 1 contained some characteristics of highly active ACE-inhibiting peptides, but the characteristics of LQPSLGFP were more conspicuous, which may be related to its molecular weight and source of mixed peptides. These findings indicated that the selenium-enriched tea mixed peptides had better potential uses than ordinary tea mixed peptides in the preparation of functional food.

CAS / MDL: 9048-46-8
研究领域: 食品科学 · 生物化学 · 药理学
✓ 已验证 产品关联 DOI 高影响因子
查看原文 查看 PubMed
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE · 2019 ·Vol. 100 ·期 1 ·315-324 · IF 2.422

Comparison of an angiotensin-I-converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

Jiali Chen,Bomi Ryu,YuanYuan Zhang,Peng Liang,Chengyong Li,Chunxia Zhou,Ping Yang,Pengzhi Hong,Zhong-Ji Qian

BACKGROUND In order to utilize tilapia skin gelatin hydrolysate protein, which is normally discarded as industrial waste in the process of fish manufacture, we study the in vivo and in vitro angiotensin-I-converting enzyme (ACE) inhibitory activity of the peptide Leu-Ser-Gly-Tyr-Gly-Pro (LSGYGP). The aim was to provide a pharmacological basis of the development of minimal side effects of ACE inhibitors by comparative analysis with captopril in molecular docking. RESULTS This peptide from protein-rich wastes showed excellent ACE inhibitory activity (IC 50 = 2.577 μmol L −1 ) and exhibited a mixed noncompetitive inhibitory pattern with Lineweaver–Burk plots. Furthermore, LSGYGP and captopril groups both showed significant decreases in blood pressure after 6 h and maintained good digestive stability over 4 h. Molecular bond interactions differentiate competitive captopril upon hydrogen bond interactions and Zn(II) interaction. The C-terminal Pro generates three interactions (hydrogen bonds, hydrophilic interactions and Van der Waals interactions) in the peptide and effectively interacts with the S1 and S2 pockets of ACE. CONCLUSION LSGYGP, with an IC 50 value of 2.577 μmol L −1 , has an antihypertensive effect in spontaneously hypertensive rats. Through comparison with captopril, this study revealed that LSGYGP may be a potential food-derived ACE inhibitory peptide and could act as a functional food ingredient to prevent hypertension. © 2019 Society of Chemical Industry

研究领域: 食品科学 · 药理学 · 生物化学
✓ 已验证 DOI PubMed 高影响因子
查看原文 查看 PubMed
Food Bioscience · 2023 · IF 5.2

Isolation, identification, and structure-activity relationship of novel ACE inhibitory peptides from earthworm protein in vitro gastrointestinal digestion product

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.

CAS / MDL: 76-05-1 76-03-9
研究领域: 生物化学 · 药理学 · 食品科学
✓ 已验证 产品关联 DOI 高影响因子
查看原文 查看 PubMed
JOURNAL OF FOOD BIOCHEMISTRY · 2021 ·Vol. 45 ·期 4 ·e13638 · IF 2.72

Dual-enzyme hydrolysis for preparation of ACE-inhibitory peptides from sesame seed protein: Optimization, separation, and identification

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.

CAS / MDL: 9001-75-6 9002-07-7
研究领域: 食品科学 · 生物化学 · 药理学
✓ 已验证 产品关联 DOI PubMed 高影响因子
查看原文 查看 PubMed
已复制

文献关联基于可获得的产品、CAS、DOI 及引用记录。收录不代表作者或出版方对阿拉丁产品的背书,请以原始文献为准。