The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis
The characterization and dynamics of protein structures upon adsorption at the air/water interface are important for understanding the mechanism of the foamability of proteins. Hydrogen–deuterium exchange, coupled with mass spectrometry (HDX-MS), is an advantageous technique for providing conformati...
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| Format: | Article |
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MDPI AG
2023-04-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/12/8/1601 |
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| author | Fei Han Qian Shen Wei Zheng Jingnan Zuo Xinyu Zhu Jingwen Li Chao Peng Bin Li Yijie Chen |
| author_facet | Fei Han Qian Shen Wei Zheng Jingnan Zuo Xinyu Zhu Jingwen Li Chao Peng Bin Li Yijie Chen |
| author_sort | Fei Han |
| collection | DOAJ |
| description | The characterization and dynamics of protein structures upon adsorption at the air/water interface are important for understanding the mechanism of the foamability of proteins. Hydrogen–deuterium exchange, coupled with mass spectrometry (HDX-MS), is an advantageous technique for providing conformational information for proteins. In this work, an air/water interface, HDX-MS, for the adsorbed proteins at the interface was developed. The model protein bovine serum albumin (BSA) was deuterium-labeled at the air/water interface in situ for different predetermined times (10 min and 4 h), and then the resulting mass shifts were analyzed by MS. The results indicated that peptides 54–63, 227–236, and 355–366 of BSA might be involved in the adsorption to the air/water interface. Moreover, the residues L55, H63, R232, A233, L234, K235, A236, R359, and V366 of these peptides might interact with the air/water interface through hydrophobic and electrostatic interactions. Meanwhile, the results showed that conformational changes of peptides 54–63, 227–236, and 355–366 could lead to structural changes in their surrounding peptides, 204–208 and 349–354, which could cause the reduction of the content of helical structures in the rearrangement process of interfacial proteins. Therefore, our air/water interface HDX-MS method could provide new and meaningful insights into the spatial conformational changes of proteins at the air/water interface, which could help us to further understand the mechanism of protein foaming properties. |
| first_indexed | 2024-03-11T05:02:21Z |
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| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-11T05:02:21Z |
| publishDate | 2023-04-01 |
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| series | Foods |
| spelling | doaj.art-aeb26adadd9a4dc4b9fcfebdbe6d03d92023-11-17T19:14:00ZengMDPI AGFoods2304-81582023-04-01128160110.3390/foods12081601The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology AnalysisFei Han0Qian Shen1Wei Zheng2Jingnan Zuo3Xinyu Zhu4Jingwen Li5Chao Peng6Bin Li7Yijie Chen8College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaNational Facility for Protein Science in Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, ChinaNational Facility for Protein Science in Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, ChinaCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaThe characterization and dynamics of protein structures upon adsorption at the air/water interface are important for understanding the mechanism of the foamability of proteins. Hydrogen–deuterium exchange, coupled with mass spectrometry (HDX-MS), is an advantageous technique for providing conformational information for proteins. In this work, an air/water interface, HDX-MS, for the adsorbed proteins at the interface was developed. The model protein bovine serum albumin (BSA) was deuterium-labeled at the air/water interface in situ for different predetermined times (10 min and 4 h), and then the resulting mass shifts were analyzed by MS. The results indicated that peptides 54–63, 227–236, and 355–366 of BSA might be involved in the adsorption to the air/water interface. Moreover, the residues L55, H63, R232, A233, L234, K235, A236, R359, and V366 of these peptides might interact with the air/water interface through hydrophobic and electrostatic interactions. Meanwhile, the results showed that conformational changes of peptides 54–63, 227–236, and 355–366 could lead to structural changes in their surrounding peptides, 204–208 and 349–354, which could cause the reduction of the content of helical structures in the rearrangement process of interfacial proteins. Therefore, our air/water interface HDX-MS method could provide new and meaningful insights into the spatial conformational changes of proteins at the air/water interface, which could help us to further understand the mechanism of protein foaming properties.https://www.mdpi.com/2304-8158/12/8/1601proteinair/water interfaceconformational changeshydrogen–deuterium exchange mass spectrometryinterfacial rheology |
| spellingShingle | Fei Han Qian Shen Wei Zheng Jingnan Zuo Xinyu Zhu Jingwen Li Chao Peng Bin Li Yijie Chen The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis Foods protein air/water interface conformational changes hydrogen–deuterium exchange mass spectrometry interfacial rheology |
| title | The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis |
| title_full | The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis |
| title_fullStr | The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis |
| title_full_unstemmed | The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis |
| title_short | The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis |
| title_sort | conformational changes of bovine serum albumin at the air water interface hdx ms and interfacial rheology analysis |
| topic | protein air/water interface conformational changes hydrogen–deuterium exchange mass spectrometry interfacial rheology |
| url | https://www.mdpi.com/2304-8158/12/8/1601 |
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