PXD007556 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Protease specificity profiling in a pipette tip using “charge-synchronized” proteome-derived peptide libraries |
Description | About 2% of the genome of human and other organisms codes for proteases. An important step toward deciphering the biological function of a protease and designing inhibitors is the profiling of protease specificity. In this work we present a novel, label-free, proteomics-based protease specificity profiling method that only requires simple sample preparation steps. It uses proteome-derived peptide libraries and enriches the cleaved sequences using strong cation exchange chromatography (SCX) material in a pipette tip. As a demonstration of the method’s versatility, we successfully determined the specificity of GluC, caspase-3, chymotrypsin and cathepsin G from several hundreds to almost 2000 cleavage events per proteases. Interestingly, we also found and confirmed a novel intrinsic preference of cathepsin G for Asn at the P1 subsite, explaining the reported cleavage position on the P. aeruginosa aeruginosa flagellin by human cathepsin G . Overall, this method is straightforward and requires so far the lowest investment in material and equipment for protease specificity profiling. Therefore, we think it will be applicable in any biochemistry laboratory and promote an increased understanding of protease specificity. |
HostingRepository | PRIDE |
AnnounceDate | 2018-04-26 |
AnnouncementXML | Submission_2018-04-26_05:56:53.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Minh Thi Nhat Nguyen |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | acetylated residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-08-28 00:57:20 | ID requested | |
⏵ 1 | 2018-04-26 05:56:54 | announced | |
Publication List
Nguyen MTN, Shema G, Zahedi RP, Verhelst SHL, Protease Specificity Profiling in a Pipet Tip Using "Charge-Synchronized" Proteome-Derived Peptide Libraries. J Proteome Res, 17(5):1923-1933(2018) [pubmed] |
Keyword List
curator keyword: Technical |
submitter keyword: ChaFRAtip, protease specificity, label-free, charged-synchronized peptide library |
Contact List
Steven L. Verhelst |
contact affiliation | Prof. Dr. Steven Verhelst Laboratory of Chemical Biology Department of Cellular and Molecular Medicine KU Leuven - University of Leuven Herestraat 49, box 802 3000 Leuven Belgium |
contact email | stevenverhelst@kuleuven.de |
lab head | |
Minh Thi Nhat Nguyen |
contact affiliation | Leibniz-Institut für Analytische Wissenschaften – ISAS – e.V. |
contact email | minh.nguyen@isas.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD007556
- Label: PRIDE project
- Name: Protease specificity profiling in a pipette tip using “charge-synchronized” proteome-derived peptide libraries