Design of a novel rhodamine B based pH-responsive magnetic adsorbent and its application in phosphopeptidomics

Protein phosphorylation is one of the most critical post-translational modifications for regulating protein activity and function. Direct mass spectrometry (MS) analysis of phosphopeptides presents significant challenges due to their inherently low abundance and the inefficient ionization characteristics. In this study, we report the design of a novel pH-responsive magnetic adsorbent, denoted as Fe<sub>3</sub>O<sub>4</sub>@NH<sub>2</sub>@Rb, for highly selective capture of phosphopeptides. This innovative material leverages dynamic and reversible electrostatic interactions between bis(2-hydroxyethyl)-3-aminopropyltriethoxysilane (Bis) and rhodamine B (Rb), which are responsive to pH changes. Under acidic conditions, Bis undergoes protonation while Rb transforms into a ring-opening zwitterionic form. The rapid and reversible transformation of Bis and Rb facilitates the efficient adsorption under acidic conditions and elution in alkaline environments. As anticipated, Fe<sub>3</sub>O<sub>4</sub>@NH<sub>2</sub>@Rb exhibits high enrichment performance for phosphopeptides from both standard protein digests and complex biological samples. This advancement holds great potential to significantly contribute to the phosphoproteomics research.

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Publication Details

Journal
Analytical Methods
Published
2025-01-01
DOI
https://doi.org/10.1039/d5ay01446h
Primary Topic
Advanced Proteomics Techniques and Applications
Type
article
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article

Design of a novel rhodamine B based pH-responsive magnetic adsorbent and its application in phosphopeptidomics

Haijiao Zheng, Jinfeng Zhang, Qiong Jia, Huifeng Zhang et al.
Analytical Methods
Advanced Proteomics Techniques and Applications
article

Design of a novel rhodamine B based pH-responsive magnetic adsorbent and its application in phosphopeptidomics

Haijiao Zheng, Jinfeng Zhang, Qiong Jia, Huifeng Zhang, Bo Hu, Shufang Yang
article en

Abstract

Protein phosphorylation is one of the most critical post-translational modifications for regulating protein activity and function. Direct mass spectrometry (MS) analysis of phosphopeptides presents significant challenges due to their inherently low abundance and the inefficient ionization characteristics. In this study, we report the design of a novel pH-responsive magnetic adsorbent, denoted as Fe<sub>3</sub>O<sub>4</sub>@NH<sub>2</sub>@Rb, for highly selective capture of phosphopeptides. This innovative material leverages dynamic and reversible electrostatic interactions between bis(2-hydroxyethyl)-3-aminopropyltriethoxysilane (Bis) and rhodamine B (Rb), which are responsive to pH changes. Under acidic conditions, Bis undergoes protonation while Rb transforms into a ring-opening zwitterionic form. The rapid and reversible transformation of Bis and Rb facilitates the efficient adsorption under acidic conditions and elution in alkaline environments. As anticipated, Fe<sub>3</sub>O<sub>4</sub>@NH<sub>2</sub>@Rb exhibits high enrichment performance for phosphopeptides from both standard protein digests and complex biological samples. This advancement holds great potential to significantly contribute to the phosphoproteomics research.

Analytical MethodsVol. 17(44)
Jilin University (CN), Jilin Jianzhu University (CN), Jilin Academy of Agricultural Sciences (CN), Apiculture Science Institute of Jinlin province (CN), Sericultural Research Institute (CN)
Openalex Percentile: Top 71%
Advanced Proteomics Techniques and Applications
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