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Motuporin

Development stage: Unknown
Modality: Peptides, Small Molecules

Overview

Motuporin is a cyclic pentapeptide natural product initially discovered in Indo-Pacific *Theonella swinhoei* sponges and also identified as a cyanobacterial toxin. It is structurally related to nodularins and microcystins, which are recognized as tumor-promoting hepatotoxins. Motuporin acts as a potent inhibitor of broad-specificity Ser/Thr protein phosphatases, specifically protein phosphatase-1 (PP-1c) and protein phosphatase-2A (PP-2Ac). A key characteristic distinguishing motuporin from microcystins is its mechanism of inhibition, which involves a non-covalent interaction with these enzymes, unlike the covalent adduct formation seen with microcystins. Laboratory synthesis of motuporin has also been achieved.

Other names: Nodularin-V

Targets

PPP2CA (Serine/threonine-protein phosphatase PP1-alpha catalytic subunit)

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