Abstract:
:A synthetic phosphonate inhibitor designed for lipase inhibition but displaying a broader range of activity was covalently immobilized on a solid support to generate a function-directed tool targeting serine hydrolases. To achieve this goal, straightforward and reliable analytical techniques were developed, allowing the monitoring of the solid support's chemical functionalization, enzyme capture processes and physisorption artifacts. This grafted inhibitor was tested on pure lipases and serine proteases from various origins, and assayed for the selective capture of lipases from several complex biological extracts. The direct identification of captured enzymes by mass spectrometry brought the proof of concept on the efficiency of this supported covalent inhibitor. The features and limitations of this "enzyme-fishing" proteomic tool provide new insight on solid-liquid inhibition process.
journal_name
Biochimiejournal_title
Biochimieauthors
Delorme V,Raux B,Puppo R,Leclaire J,Cavalier JF,Marc S,Kamarajugadda PK,Buono G,Fotiadu F,Canaan S,Carrière Fdoi
10.1016/j.biochi.2014.07.015subject
Has Abstractpub_date
2014-12-01 00:00:00pages
124-34eissn
0300-9084issn
1638-6183pii
S0300-9084(14)00206-5journal_volume
107 Pt Apub_type
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