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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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Autores principales: Han, Fei, Shen, Qian, Zheng, Wei, Zuo, Jingnan, Zhu, Xinyu, Li, Jingwen, Peng, Chao, Li, Bin, Chen, Yijie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10137346/
https://www.ncbi.nlm.nih.gov/pubmed/37107396
http://dx.doi.org/10.3390/foods12081601
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author Han, Fei
Shen, Qian
Zheng, Wei
Zuo, Jingnan
Zhu, Xinyu
Li, Jingwen
Peng, Chao
Li, Bin
Chen, Yijie
author_facet Han, Fei
Shen, Qian
Zheng, Wei
Zuo, Jingnan
Zhu, Xinyu
Li, Jingwen
Peng, Chao
Li, Bin
Chen, Yijie
author_sort Han, Fei
collection PubMed
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.
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spelling pubmed-101373462023-04-28 The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis Han, Fei Shen, Qian Zheng, Wei Zuo, Jingnan Zhu, Xinyu Li, Jingwen Peng, Chao Li, Bin Chen, Yijie Foods Article 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. MDPI 2023-04-10 /pmc/articles/PMC10137346/ /pubmed/37107396 http://dx.doi.org/10.3390/foods12081601 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Han, Fei
Shen, Qian
Zheng, Wei
Zuo, Jingnan
Zhu, Xinyu
Li, Jingwen
Peng, Chao
Li, Bin
Chen, Yijie
The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis
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 Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10137346/
https://www.ncbi.nlm.nih.gov/pubmed/37107396
http://dx.doi.org/10.3390/foods12081601
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