دورية أكاديمية
A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution.
| العنوان: | A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution. |
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| المؤلفون: | Meng P; State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products and School of Marine Science, Ningbo University, Ningbo 315211, China., Wang Y; State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products and School of Marine Science, Ningbo University, Ningbo 315211, China., Huang Y; State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products and School of Marine Science, Ningbo University, Ningbo 315211, China., Liu T; State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products and School of Marine Science, Ningbo University, Ningbo 315211, China., Ma M; State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products and School of Marine Science, Ningbo University, Ningbo 315211, China., Han J; State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products and School of Marine Science, Ningbo University, Ningbo 315211, China., Su X; State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products and School of Marine Science, Ningbo University, Ningbo 315211, China., Li W; Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai 264003, China. Electronic address: wjli@yic.ac.cn., Wang Y; Food Safety Key Laboratory of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China; School of Food and Health, Beijing Technology and Business University, Beijing 100048, China., Lu C; State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products and School of Marine Science, Ningbo University, Ningbo 315211, China; Food Safety Key Laboratory of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China. Electronic address: luchenyang@nbu.edu.cn. |
| المصدر: | Food chemistry [Food Chem] 2024 Jun 01; Vol. 442, pp. 138401. Date of Electronic Publication: 2024 Jan 12. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Applied Science Publishers Country of Publication: England NLM ID: 7702639 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-7072 (Electronic) Linking ISSN: 03088146 NLM ISO Abbreviation: Food Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Barking : Elsevier Applied Science Publishers Original Publication: Barking, Eng., Applied Science Publishers. |
| مواضيع طبية MeSH: | Xanthine Oxidase* , Peptidyl-Dipeptidase A*, Molecular Docking Simulation ; Uric Acid ; Peptides/pharmacology ; Enzyme Inhibitors/pharmacology ; Enzyme Inhibitors/chemistry |
| مستخلص: | Molecular docking and activity evaluation screened the dipeptide module GP with low xanthine oxidase (XOD) inhibitory activity and modules KE and KN with high activity, and identified them as low- and high-contribution modules, respectively. We hypothesized the substitution of low-contribution modules in peptides with high contributions would boost their XOD inhibitory activity. In the XOD inhibitory peptide GPAGPR, substitution of GP with both KE and KN led to enhanced affinity between the peptides and XOD. They also increased XOD inhibitory activity (26.4% and 10.3%) and decreased cellular uric acid concentrations (28.0% and 10.4%). RNA sequencing indicated that these improvements were attributable to the inhibition of uric acid biosynthesis. In addition, module substitution increased the angiotensin-converting enzyme inhibitory activity of GILRP and GAAGGAF by 84.8% and 76.5%. This study revealed that module substitution is a feasible strategy to boost peptide activity, and provided information for the optimization of hydrolysate preparation conditions. Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (Copyright © 2024 Elsevier Ltd. All rights reserved.) |
| فهرسة مساهمة: | Keywords: Activity boosting strategy; Angiotensin-converting enzyme inhibitory; Module substitution; Molecular docking; Peptide; Xanthine oxidase inhibitory |
| المشرفين على المادة: | EC 1.17.3.2 (Xanthine Oxidase) EC 3.4.15.1 (Peptidyl-Dipeptidase A) 268B43MJ25 (Uric Acid) 0 (Peptides) 0 (Enzyme Inhibitors) |
| تواريخ الأحداث: | Date Created: 20240114 Date Completed: 20240214 Latest Revision: 20240214 |
| رمز التحديث: | 20240214 |
| DOI: | 10.1016/j.foodchem.2024.138401 |
| PMID: | 38219570 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1873-7072 |
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| DOI: | 10.1016/j.foodchem.2024.138401 |