Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak Cheese
In this study, the physicochemical properties of two bitter peptides derived from yak cheese, RPKHPIK (RK7) and KVLPVPQ (KQ7) were calculated by using online bioinformatics tools such as ExPASy-ProtParam, Innovagen, and Pep-Draw. Molecular docking was used to elucidate the mechanism of the inhibitor...
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| Format: | Article |
| Language: | English |
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China Food Publishing Company
2023-01-01
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| Series: | Shipin Kexue |
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| Online Access: | https://www.spkx.net.cn/fileup/1002-6630/PDF/2023-44-2-018.pdf |
| _version_ | 1811159483107246080 |
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| author | LI Mengyao, LIANG Qi, SONG Xuemei |
| author_facet | LI Mengyao, LIANG Qi, SONG Xuemei |
| author_sort | LI Mengyao, LIANG Qi, SONG Xuemei |
| collection | DOAJ |
| description | In this study, the physicochemical properties of two bitter peptides derived from yak cheese, RPKHPIK (RK7) and KVLPVPQ (KQ7) were calculated by using online bioinformatics tools such as ExPASy-ProtParam, Innovagen, and Pep-Draw. Molecular docking was used to elucidate the mechanism of the inhibitory effect of the two peptides on α-amylase and their α-amylase inhibitory activity was determined. The results showed that the molecular masses of RK7 and KQ7 were 875.07 and 779.98 Da, and their hydrophobicity were 42.86% and 71.42%, respectively. Molecular docking showed that His305, Glu233, Trp59 and Trp58 in α-amylase played an important role in binding to RK7 and KQ7. Furthermore, Asp197, Glu233 and Asp300 were the key amino acids for the activity of α-amylase. The half maximal inhibitory concentration (IC50) of RK7 and KQ7 against α-amylase were 0.45 and 0.86 mg/mL, respectively. The findings of this study provide new evidence for the study of α-amylase inhibitory peptides. |
| first_indexed | 2024-04-10T05:42:58Z |
| format | Article |
| id | doaj.art-376ca437832e445a91512fdf7e5189b1 |
| institution | Directory Open Access Journal |
| issn | 1002-6630 |
| language | English |
| last_indexed | 2024-04-10T05:42:58Z |
| publishDate | 2023-01-01 |
| publisher | China Food Publishing Company |
| record_format | Article |
| series | Shipin Kexue |
| spelling | doaj.art-376ca437832e445a91512fdf7e5189b12023-03-06T07:13:02ZengChina Food Publishing CompanyShipin Kexue1002-66302023-01-0144213213810.7506/spkx1002-6630-20220120-197Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak CheeseLI Mengyao, LIANG Qi, SONG Xuemei0(1. College of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, China;2. Functional Dairy Product Engineering Laboratory of Gansu, Lanzhou 730070, China)In this study, the physicochemical properties of two bitter peptides derived from yak cheese, RPKHPIK (RK7) and KVLPVPQ (KQ7) were calculated by using online bioinformatics tools such as ExPASy-ProtParam, Innovagen, and Pep-Draw. Molecular docking was used to elucidate the mechanism of the inhibitory effect of the two peptides on α-amylase and their α-amylase inhibitory activity was determined. The results showed that the molecular masses of RK7 and KQ7 were 875.07 and 779.98 Da, and their hydrophobicity were 42.86% and 71.42%, respectively. Molecular docking showed that His305, Glu233, Trp59 and Trp58 in α-amylase played an important role in binding to RK7 and KQ7. Furthermore, Asp197, Glu233 and Asp300 were the key amino acids for the activity of α-amylase. The half maximal inhibitory concentration (IC50) of RK7 and KQ7 against α-amylase were 0.45 and 0.86 mg/mL, respectively. The findings of this study provide new evidence for the study of α-amylase inhibitory peptides.https://www.spkx.net.cn/fileup/1002-6630/PDF/2023-44-2-018.pdfyak cheese; bitter peptide; α-amylase inhibitory activity; molecular docking; mechanism of action |
| spellingShingle | LI Mengyao, LIANG Qi, SONG Xuemei Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak Cheese Shipin Kexue yak cheese; bitter peptide; α-amylase inhibitory activity; molecular docking; mechanism of action |
| title | Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak Cheese |
| title_full | Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak Cheese |
| title_fullStr | Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak Cheese |
| title_full_unstemmed | Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak Cheese |
| title_short | Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak Cheese |
| title_sort | using molecular docking to investigate the alpha amylase inhibitory activity of bitter peptides rk7 and kq7 derived from yak cheese |
| topic | yak cheese; bitter peptide; α-amylase inhibitory activity; molecular docking; mechanism of action |
| url | https://www.spkx.net.cn/fileup/1002-6630/PDF/2023-44-2-018.pdf |
| work_keys_str_mv | AT limengyaoliangqisongxuemei usingmoleculardockingtoinvestigatethealphaamylaseinhibitoryactivityofbitterpeptidesrk7andkq7derivedfromyakcheese |