The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis
文献类型： 外文期刊
作者： Han, Fei 1 ; Shen, Qian 1 ; Zheng, Wei 1 ; Zuo, Jingnan 1 ; Zhu, Xinyu 1 ; Li, Jingwen 2 ; Peng, Chao 2 ; Li, Bin 1 ; Chen, Yijie 1 ;
作者机构： 1.Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Peoples R China
2.Chinese Acad Sci, Shanghai Adv Res Inst, Natl Facil Prot Sci Shanghai, Shanghai 201210, Peoples R China
3.Huazhong Agr Univ, Shenzhen Inst Nutr & Hlth, Wuhan 430070, Peoples R China
4.Chinese Acad Agr Sci, Agr Genom Inst Shenzhen, Genome Anal Lab, Minist Agr, Shenzhen 518124, Peoples R China
关键词： protein; air; water interface; conformational changes; hydrogen-deuterium exchange mass spectrometry; interfacial rheology
期刊名称：FOODS （ 影响因子：5.2； 五年影响因子：5.5 ）
ISSN：
年卷期： 2023 年 12 卷 8 期
页码：
收录情况： SCI
摘要： 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.
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