Biofunctionalized dissolvable hydrogel microbeads enable efficient characterization of native protein complexes

The characterization of protein complex is vital for unraveling biological mechanisms in various life processes. Despite advancements in biophysical tools, the capture of non-covalent complexes and deciphering of their biochemical composition continue to present challenges for low-input samples. Here we introduce SNAP-MS, a Stationary-phase-dissolvable Native Affinity Purification and Mass Spectrometric characterization strategy. It allows for highly efficient purification and characterization from inputs at the pico-mole level. SNAP-MS replaces traditional elution with matrix dissolving during the recovery of captured targets, enabling the use of high-affinity bait-target pairs and eliminates interstitial voids. The purified intact protein complexes are compatible with native MS, which provides structural information including stoichiometry, topology, and distribution of proteoforms, size variants and interaction states. An algorithm utilizes the bait as a charge remover and mass corrector significantly enhances the accuracy of analyzing heterogeneously glycosylated complexes. With a sample-to-data time as brief as 2 hours, SNAP-MS demonstrates considerable versatility in characterizing native complexes from biological samples, including blood samples.

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Publication Details

Journal
Nature Communications
Published
2024-10-05
DOI
https://doi.org/10.1038/s41467-024-52948-5
Citations
5
Primary Topic
Mass Spectrometry Techniques and Applications
Type
article
Field-Weighted Citation Impact
1.20

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article

Biofunctionalized dissolvable hydrogel microbeads enable efficient characterization of native protein complexes

Ye Tian, Yanxi Zhu, Haifeng Duan, Guanbo Wang et al.
5 citations
Nature Communications
Mass Spectrometry Techniques and Applications
1.20
article

Biofunctionalized dissolvable hydrogel microbeads enable efficient characterization of native protein complexes

Ye Tian, Yanxi Zhu, Haifeng Duan, Guanbo Wang, Lingxiao Chaihu, Junlong Yin, Yanyi Huang, Xinyang Shao, Minjie Tan, Hongwei Wang, Jianbin Wang, Meng Tian, Ziwei Wang, Changsheng Xia, Hui Wang, Yifan Wang
article en
5 citations

Abstract

The characterization of protein complex is vital for unraveling biological mechanisms in various life processes. Despite advancements in biophysical tools, the capture of non-covalent complexes and deciphering of their biochemical composition continue to present challenges for low-input samples. Here we introduce SNAP-MS, a Stationary-phase-dissolvable Native Affinity Purification and Mass Spectrometric characterization strategy. It allows for highly efficient purification and characterization from inputs at the pico-mole level. SNAP-MS replaces traditional elution with matrix dissolving during the recovery of captured targets, enabling the use of high-affinity bait-target pairs and eliminates interstitial voids. The purified intact protein complexes are compatible with native MS, which provides structural information including stoichiometry, topology, and distribution of proteoforms, size variants and interaction states. An algorithm utilizes the bait as a charge remover and mass corrector significantly enhances the accuracy of analyzing heterogeneously glycosylated complexes. With a sample-to-data time as brief as 2 hours, SNAP-MS demonstrates considerable versatility in characterizing native complexes from biological samples, including blood samples.

Nature CommunicationsVol. 15(1)
Nanjing Normal University (CN), Peking University (CN), Beijing Biocytogen (China) (CN), Shenzhen Bay Laboratory (CN), Beijing National Laboratory for Molecular Sciences (CN), Peking University People's Hospital (CN), Beijing Tsinghua Chang Gung Hospital (CN), Center for Life Sciences (CN), Tsinghua University (CN)
National Natural Science Foundation of China, Peking University, National Health Commission of the People's Republic of China
Responsible consumption and production
Openalex Percentile: Top 23%
Mass Spectrometry Techniques and Applications
1.20
DOIOpen Access PDFOpenAlex
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