ArticleScientific reports2026
A protein-small molecule conjugate as a bispecific inhibitor of proteases implicated in cancer metastasis.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Matrix metalloproteinase-9 (MMP-9) and kallikrein 6 (KLK6) are key extracellular proteases implicated in metastatic progression. In colorectal and pancreatic cancers, their overexpression correlates with aggressive disease and poor prognosis, making them attractive therapeutic targets. While monospecific inhibition of either protease shows limited efficacy, simultaneous dual inhibition has not yet been explored as a strategy to block metastasis. To address the lack of an efficient inhibitor of the above metastatic cancers, we prepared a bispecific inhibitor by the site-specific conjugation, via click chemistry, of a selective inhibitor of MMP-9 to a small molecule specifically inhibiting KLK6; the inhibitor comprised the N-terminal domain of tissue inhibitor of metalloproteinases 2 (N-TIMP2), bearing the non-canonical amino acid propargyl lysine (PrK), conjugated to a small molecule known as DKFZ-938. The bispecific inhibitor, thus designated N-TIMP2
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