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van de Plassche, M.A.T.* ; O'Neill, T.J. ; Seeholzer, T. ; Turk, B.* ; Krappmann, D. ; Verhelst, S.H.L.*

Use of non-natural amino acids for the design and synthesis of a selective, cell-permeable MALT1 activity-based probe.

J. Med. Chem. 63, 3996-4004 (2020)

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	Open Access Green

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Constitutive proteolytic activity of MALT1 is associated with highly aggressive B-cell lymphomas. Chemical tools that detect active MALT1 have been reported, but suffer from poor cell permeability and/or cross-reactivity with the cysteine protease cathepsin B. Here, we report that the non-natural amino acid pipecolinic acid in the P2 position of substrates and chemical probes leads to improved selectivity toward MALT1 and results in cell-permeable fluorescent probes.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Protease; Paracaspase; Specificity; Activation

ISSN (print) / ISBN 0022-2623

e-ISSN 1520-4804

Journal Journal of Medicinal Chemistry

Quellenangaben Volume: 63, Issue: 8, Pages: 3996-4004

Publisher American Chemical Society (ACS)

Publishing Place 1155 16th St, Nw, Washington, Dc 20036 Usa

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Research Unit Signaling and Translation (SAT)