Inhibition of Iron Release from Donkey Spleen Ferritin through Malt-Derived Protein Z–Ferulic Acid Interactions
Protein–small molecule interactions naturally occur in foodstuffs, which could improve the properties of protein and small molecules. Meanwhile, they might affect the bioavailability and nutritional value of proteins. Ferritin, as an iron-storage protein, has been a focus of research. However, the c...
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MDPI AG
2023-01-01
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Online Access: | https://www.mdpi.com/2304-8158/12/2/234 |
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author | Mingyang Sun Hanhan Liu Chen Xu Zhenghui Jiang Chenyan Lv |
author_facet | Mingyang Sun Hanhan Liu Chen Xu Zhenghui Jiang Chenyan Lv |
author_sort | Mingyang Sun |
collection | DOAJ |
description | Protein–small molecule interactions naturally occur in foodstuffs, which could improve the properties of protein and small molecules. Meanwhile, they might affect the bioavailability and nutritional value of proteins. Ferritin, as an iron-storage protein, has been a focus of research. However, the complexity of foodstuffs enables the interaction between ferritin and food components, especially polyphenols, which can induce iron release from ferritin. Thus, the application of ferritin in food is limited. Inspired by the natural-occurring, strong protein–polyphenol interactions in beer, to inhibit the iron release of ferritin, the malt-derived protein Z (PZ) was chosen to interact with ferulic acid (FA), an abundant reductant in malt, beer, and other foodstuffs. The analysis of the interaction between PZ and FA was carried out using fluorescence spectroscopy, the results of which suggest that one PZ molecule can bind with 22.11 ± 2.13 of FA, and the binding constant is (4.99 ± 2.13) × 10<sup>5</sup> M<sup>−1</sup>. In a molecular dynamics (MD) simulation, FA was found to be embedded in the internal hydrophobic pocket of PZ, where it formed hydrogen bonds with Val-389 and Tyr-234. As expected, compared to iron release induced by FA, the iron release from donkey spleen ferritin (DSF) induced by FA decreased by 86.20% in the presence of PZ. Meanwhile, based on the PZ–FA interaction, adding PZ in beer reduced iron release from DSF by 40.5% when DSF:PZ was 1:40 (molar ratio). This work will provide a novel method of inhibiting iron release from ferritin. |
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language | English |
last_indexed | 2024-03-09T12:45:24Z |
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series | Foods |
spelling | doaj.art-f9896af0c27742acb769414d9ed00cd82023-11-30T22:13:21ZengMDPI AGFoods2304-81582023-01-0112223410.3390/foods12020234Inhibition of Iron Release from Donkey Spleen Ferritin through Malt-Derived Protein Z–Ferulic Acid InteractionsMingyang Sun0Hanhan Liu1Chen Xu2Zhenghui Jiang3Chenyan Lv4College of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing 100083, ChinaCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing 100083, ChinaCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing 100083, ChinaCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing 100083, ChinaCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing 100083, ChinaProtein–small molecule interactions naturally occur in foodstuffs, which could improve the properties of protein and small molecules. Meanwhile, they might affect the bioavailability and nutritional value of proteins. Ferritin, as an iron-storage protein, has been a focus of research. However, the complexity of foodstuffs enables the interaction between ferritin and food components, especially polyphenols, which can induce iron release from ferritin. Thus, the application of ferritin in food is limited. Inspired by the natural-occurring, strong protein–polyphenol interactions in beer, to inhibit the iron release of ferritin, the malt-derived protein Z (PZ) was chosen to interact with ferulic acid (FA), an abundant reductant in malt, beer, and other foodstuffs. The analysis of the interaction between PZ and FA was carried out using fluorescence spectroscopy, the results of which suggest that one PZ molecule can bind with 22.11 ± 2.13 of FA, and the binding constant is (4.99 ± 2.13) × 10<sup>5</sup> M<sup>−1</sup>. In a molecular dynamics (MD) simulation, FA was found to be embedded in the internal hydrophobic pocket of PZ, where it formed hydrogen bonds with Val-389 and Tyr-234. As expected, compared to iron release induced by FA, the iron release from donkey spleen ferritin (DSF) induced by FA decreased by 86.20% in the presence of PZ. Meanwhile, based on the PZ–FA interaction, adding PZ in beer reduced iron release from DSF by 40.5% when DSF:PZ was 1:40 (molar ratio). This work will provide a novel method of inhibiting iron release from ferritin.https://www.mdpi.com/2304-8158/12/2/234ferritinprotein Zinteractionferulic acidiron release |
spellingShingle | Mingyang Sun Hanhan Liu Chen Xu Zhenghui Jiang Chenyan Lv Inhibition of Iron Release from Donkey Spleen Ferritin through Malt-Derived Protein Z–Ferulic Acid Interactions Foods ferritin protein Z interaction ferulic acid iron release |
title | Inhibition of Iron Release from Donkey Spleen Ferritin through Malt-Derived Protein Z–Ferulic Acid Interactions |
title_full | Inhibition of Iron Release from Donkey Spleen Ferritin through Malt-Derived Protein Z–Ferulic Acid Interactions |
title_fullStr | Inhibition of Iron Release from Donkey Spleen Ferritin through Malt-Derived Protein Z–Ferulic Acid Interactions |
title_full_unstemmed | Inhibition of Iron Release from Donkey Spleen Ferritin through Malt-Derived Protein Z–Ferulic Acid Interactions |
title_short | Inhibition of Iron Release from Donkey Spleen Ferritin through Malt-Derived Protein Z–Ferulic Acid Interactions |
title_sort | inhibition of iron release from donkey spleen ferritin through malt derived protein z ferulic acid interactions |
topic | ferritin protein Z interaction ferulic acid iron release |
url | https://www.mdpi.com/2304-8158/12/2/234 |
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