数字农科院2.0

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： Fei Han;Qian Shen;Wei Zheng;Jingnan Zuo;Xinyu Zhu;Jingwen Li;Chao Peng;Bin Li;Yijie Chen

作者机构：

关键词： air/water interface;conformational changes;hydrogen–deuterium exchange mass spectrometry;interfacial rheology;protein

期刊名称： Foods

ISSN： 2304-8158

年卷期： 2023 年 12 卷 8 期

页码：

收录情况： SCIE（2023版）

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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