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Here, we present an enrichment\u2010free chemoproteomic approach that enables direct mass spectrometric detection by Matrix\u2010Assisted Laser Desorption\/Ionization (MALDI) of active proteases. An active\u2010site\u2013directed affinity probe transfers, through a proximity\u2010induced reaction, a MALDI\u2010detectable \u03b1\u2010cyano\u20104\u2010hydroxycinnamic acid (CHCA) tag exclusively to catalytically active forms of matrix metalloproteases (MMPs). The CHCA label enhances ionization efficiency and markedly improves signal\u2010to\u2010noise ratios, allowing confident identification of CHCA\u2010labelled peptides under discriminating analytical conditions. Each active metalloprotease is thereby, associated with a distinct set of CHCA signature peptides, defining its activity fingerprint. This workflow achieves multiplexed and quantitative activity profiling of MMPs, directly in complex proteomes. This design expands ABPP into the mass spectrometry domain and establishes a robust platform for activity\u2010based enzyme detection.<\/jats:p>","DOI":"10.1002\/anie.202523132","type":"journal-article","created":{"date-parts":[[2026,4,4]],"date-time":"2026-04-04T08:24:17Z","timestamp":1775291057000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Proximity\u2010Induced Transfer of a Mass Tag Enables Direct Profiling of Active Matrix Metalloproteases"],"prefix":"10.1002","volume":"65","author":[{"given":"Lomane","family":"Berthy","sequence":"first","affiliation":[{"name":"CEA, INRAE, M\u00e9dicaments et Technologies pour La Sant\u00e9 (MTS), SIMoS Universit\u00e9 Paris\u2010Saclay  Gif\u2010sur\u2010Yvette France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ugo","family":"Pasco","sequence":"additional","affiliation":[{"name":"IBMM, Univ. 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