Protein phosphorylation is one of the most important post-translational modifications.It is an active research area to study phosphoproteomics for discovery of disease biomarkers and druggable targets.Here we report t...Protein phosphorylation is one of the most important post-translational modifications.It is an active research area to study phosphoproteomics for discovery of disease biomarkers and druggable targets.Here we report the development of superparamagnetic Fe_(3)O_(4)@mZrO_(2) core-shell microspheres with mesoporous structures for highly efficient enrichment of phosphopeptides.We have demonstrated that the mesoporous ZrO_(2) layer dramatically improves the selective enrichment of phosphopeptides.Our approach allows for in-situ elution and sensitive identification of both mono-phosphorylated and multiphosphorylated peptides in MALDI-TOF mass spectrometry,with the detection limit of down to the femtomole range.The target phosphopeptides can reliably be enriched for MS analysis from various complex samples including the spiked protein digests and tumor cell lysates.The Fe_(3)O_(4)@mZrO_(2) coreshell microspheres promise a useful tool for phosphoproteomics by allowing for highly efficient and selective enrichment of the crucial signaling regulators in a low abundance.展开更多
基金supported by the National Key Research and Development Program of China(2017YFE0131700)and the National Natural Science Foundation of China(21874096)+3 种基金a project supported by Collaborative Innovation Center of Suzhou Nano Science and Technologythe 111 ProjectJoint International Research Laboratory of Carbon-Based Functional Materials and Devicesthe Priority Academic Program Development of Jiangsu Higher Education Institutions(PAPD)。
文摘Protein phosphorylation is one of the most important post-translational modifications.It is an active research area to study phosphoproteomics for discovery of disease biomarkers and druggable targets.Here we report the development of superparamagnetic Fe_(3)O_(4)@mZrO_(2) core-shell microspheres with mesoporous structures for highly efficient enrichment of phosphopeptides.We have demonstrated that the mesoporous ZrO_(2) layer dramatically improves the selective enrichment of phosphopeptides.Our approach allows for in-situ elution and sensitive identification of both mono-phosphorylated and multiphosphorylated peptides in MALDI-TOF mass spectrometry,with the detection limit of down to the femtomole range.The target phosphopeptides can reliably be enriched for MS analysis from various complex samples including the spiked protein digests and tumor cell lysates.The Fe_(3)O_(4)@mZrO_(2) coreshell microspheres promise a useful tool for phosphoproteomics by allowing for highly efficient and selective enrichment of the crucial signaling regulators in a low abundance.
