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A New Affinity-Based Probe to Profile MMP Active Forms

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Proteases and Cancer

Abstract

A new generation of affinity-based probes (AfBPs) has been developed to label and identity matrix metalloproteinases (MMPs) under their active form in complex proteomes. First, the probe reacts with an active MMP through a proximity-driven reaction that does not require any external trigger. Following this affinity-labeling step, a streptavidin-based enrichment of the resulting biotin-tagged MMP is carried out. Finally, after on-beads proteolytic digestion by trypsin, MMP signature peptides are analyzed and identified by mass spectrometry. Such a “photoactivation-free” labeling can be applied to the detection of several MMPs in a wide variety of biological systems, including in vivo conditions.

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Acknowledgments

This work was supported by the French National Research Agency (ANR-18-CE44-0012).

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Correspondence to Laurent Devel .

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© 2024 The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature

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Malgorn, C. et al. (2024). A New Affinity-Based Probe to Profile MMP Active Forms. In: Santamaria, S. (eds) Proteases and Cancer. Methods in Molecular Biology, vol 2747. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-3589-6_3

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  • DOI: https://doi.org/10.1007/978-1-0716-3589-6_3

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-3588-9

  • Online ISBN: 978-1-0716-3589-6

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