Proteomics

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In-depth Endogenous Phosphopeptidomics of Serum with Zirconium (IV)-Grafted Mesoporous Silica Enrichment

ABSTRACT: In this study, we developed an approach using Zirconium (IV)-grafted mesoporous beads to enrich phosphopeptides followed by analysis with a high resolution nanoRPLC-MS/MS system. The new method was first tested with tryptic digests of standard phosphoproteins and HeLa cell lysates, with excellent enrichment performance achieved. The method was further used for endogenous phosphopeptidomic analysis of serum samples from pancreatic ductal adenocarcinoma (PDAC) patients and controls. In total, 329 endogenous phosphopeptides (containing 113 high confidence sites) were identified across samples, by far the largest endogenous phosphorylation dataset catalogued to date. In addition, the method was readily applied for phosphoproteomics of the same set of samples, with 172 phosphopeptides identified and significant changes in dozens of phosphopeptides observed. Taken together, this method serves as a benchmark for analyzing serum phosphorylation events. Given the simplicity and robustness of the proposed method, we envision that it can be readily used for comprehensive phosphorylation studies (i.e., simultaneous endogenous phosphopeptidomics and phosphoproteomics) of serum and other biofluid samples.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Blood Serum

SUBMITTER: Ci Wu  

LAB HEAD: Ci Wu

PROVIDER: PXD045146 | Pride | 2024-06-16

REPOSITORIES: Pride

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Hela_pST_MCM48_L2_02.msf Msf
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Hela_pST_MCM48_L2_03.msf Msf
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In-Depth Endogenous Phosphopeptidomics of Serum with Zirconium(IV)-Grafted Mesoporous Silica Enrichment.

Wu Ci C   Zhang Shen S   Hou Chunyan C   Byers Stephen S   Ma Junfeng J  

Analytical chemistry 20240510 21

Detection of endogenous peptides, especially those with modifications (such as phosphorylation) in biofluids, can serve as an indicator of intracellular pathophysiology. Although great progress has been made in phosphoproteomics in recent years, endogenous phosphopeptidomics has largely lagged behind. One main hurdle in endogenous phosphopeptidomics analysis is the coexistence of proteins and highly abundant nonmodified peptides in complex matrices. In this study, we developed an approach using  ...[more]

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