PXD037549 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Cotton Ti-IMAC: Developing Phosphorylated Cotton as a Novel Platform for Phosphopeptide Enrichment |
Description | Protein phosphorylation is one of the most common post-translational modifications (PTMs), which is involved in many important physiological functions. Understanding protein phosphorylation at molecular level is critical to decipher its relevant biological processes and signaling networks. Mass spectrometry (MS) has been proved to be a powerful tool in comprehensive characterization of protein phosphorylation. Yet the low abundance and poor ionization efficiency of phosphopeptides make its MS analysis challenging; an enrichment with high efficiency and selectivity is always necessary before MS analysis. In this study, we developed a phosphorylated cotton fiber-based Ti(IV)-IMAC material (termed as: Cotton Ti-IMAC) that can serve as a novel platform for phosphopeptide enrichment. The cotton fiber can be effectively grafted with phosphate groups in a single step, where the titanium ions can then be immobilized onto to capture phosphopeptides. The material can be prepared with cost-effective reagents within only 4 hours. Benefiting from the flexibility and filterability of cotton fibers, the material can be easily packed as a spin-tip and make the enrichment process more convenient. Cotton Ti-IMAC successfully enriched phosphopeptides from protein standard digests and exhibited a high selectivity (β-casein/BSA = 1:1000) and excellent sensitivity (0.1 fmol/µL). Moreover, 2354 phosphopeptides was identified in a single LC-MS/MS injection after enriching from only 100 µg HeLa cell digests, with an enrichment specificity up to 97.51%. Taken together, we believe Cotton Ti-IMAC is ready to serve as a widely applicable and robust platform for achieving large-scale phosphopeptide enrichment and expanding our knowledge of phosphoproteomics in complex biological systems. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_08:24:08.568.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Danqing Wang |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | phosphorylated residue |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-10-19 02:39:47 | ID requested | |
1 | 2023-10-23 13:49:36 | announced | |
⏵ 2 | 2023-11-14 08:24:08 | announced | 2023-11-14: Updated project metadata. |
3 | 2024-10-22 06:07:14 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Phosphoproteomics, LC-MS/MS |
Contact List
Lingjun Li |
contact affiliation | Department of Chemistry and School of Pharmacy, University of Wisconsin-Madison |
contact email | lingjun.li@wisc.edu |
lab head | |
Danqing Wang |
contact affiliation | University of Wisconsin-Madison |
contact email | dwang356@wisc.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD037549
- Label: PRIDE project
- Name: Cotton Ti-IMAC: Developing Phosphorylated Cotton as a Novel Platform for Phosphopeptide Enrichment