Cargando…
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...
Autores principales: | , , , , , , , , |
---|---|
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 |
_version_ | 1785032440731926528 |
---|---|
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. |
format | Online Article Text |
id | pubmed-10137346 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT hanfei theconformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT shenqian theconformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT zhengwei theconformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT zuojingnan theconformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT zhuxinyu theconformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT lijingwen theconformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT pengchao theconformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT libin theconformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT chenyijie theconformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT hanfei conformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT shenqian conformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT zhengwei conformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT zuojingnan conformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT zhuxinyu conformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT lijingwen conformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT pengchao conformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT libin conformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis AT chenyijie conformationalchangesofbovineserumalbuminattheairwaterinterfacehdxmsandinterfacialrheologyanalysis |