دورية أكاديمية
Analyzing noncovalent interactions between notoginseng saponins and lysozyme by deposition scanning intensity fading MALDI-TOF mass spectrometry.
| العنوان: | Analyzing noncovalent interactions between notoginseng saponins and lysozyme by deposition scanning intensity fading MALDI-TOF mass spectrometry. |
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| المؤلفون: | Zhao X; Key Laboratory for Applied Technology of Sophisticated Analytical Instruments, Shandong Analysis and Test Centre, Qilu University of Technology (Shandong Academy of Sciences), Jinan, China., Ren J; Department of Pharmaceutical Science, Zunyi Medical University at Zhuhai Campus, Zhuhai, China., Wang Z; Department of Pharmaceutical Science, Zunyi Medical University at Zhuhai Campus, Zhuhai, China., Chen X; Key Laboratory for Applied Technology of Sophisticated Analytical Instruments, Shandong Analysis and Test Centre, Qilu University of Technology (Shandong Academy of Sciences), Jinan, China. |
| المصدر: | Journal of mass spectrometry : JMS [J Mass Spectrom] 2024 Jul; Vol. 59 (7), pp. e5058. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Wiley Country of Publication: England NLM ID: 9504818 Publication Model: Print Cited Medium: Internet ISSN: 1096-9888 (Electronic) Linking ISSN: 10765174 NLM ISO Abbreviation: J Mass Spectrom Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Chichester, UK : Wiley, c1995- |
| مواضيع طبية MeSH: | Muramidase*/chemistry , Muramidase*/metabolism , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization*/methods , Saponins*/chemistry , Saponins*/analysis , Saponins*/metabolism , Panax notoginseng*/chemistry, Protein Binding ; Molecular Docking Simulation ; Reproducibility of Results ; Animals ; Trisaccharides |
| مستخلص: | Analysis of noncovalent interactions between natural products and proteins is important for rapid screening of active ingredients and understanding their pharmacological activities. In this work, the intensity fading MALDI-TOF mass spectrometry (IF-MALDI-MS) method with improved reproducibility was implemented to investigate the binding interactions between saponins from Panax notoginseng and lysozyme. The benchmark IF-MALDI-MS experiment was established using N,N',N″-triacetylchitotriose-lysozyme as a model system. The reproducibility of ion intensities in IF-MALDI-MS was improved by scanning the whole sample deposition with a focused laser beam. The relative standard deviation (RSD) of deposition scanning IF-MALDI-MS is 5.7%. Similar decay trends of the relative intensities of notoginseng saponins against increasing amounts of lysozyme were observed for all six notoginseng saponins. The half-maximal fading concentration (FC (© 2024 John Wiley & Sons Ltd.) |
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| معلومات مُعتمدة: | 81860617 National Natural Science Foundation of China; 22074071 National Natural Science Foundation of China; 32360117 National Natural Science Foundation of China; tsqn202103099 Program for Taishan Scholars of Shandong Province; QKH-J[2020]1Y045 Guizhou Provincial Natural Science Foundation; 2021GXRC090 Jinan University and Institute Innovation Team Project |
| فهرسة مساهمة: | Keywords: MALDI‐MS; Panax notoginseng; intensity fading; lysozyme; molecular docking; noncovalent interaction |
| المشرفين على المادة: | EC 3.2.1.17 (Muramidase) 0 (Saponins) 38864-21-0 (N,N',N''-triacetylchitotriose) 0 (Trisaccharides) |
| تواريخ الأحداث: | Date Created: 20240606 Date Completed: 20240606 Latest Revision: 20240617 |
| رمز التحديث: | 20240617 |
| DOI: | 10.1002/jms.5058 |
| PMID: | 38842112 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1096-9888 |
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| DOI: | 10.1002/jms.5058 |