Supramolecular control of enzyme activity through cucurbit[8]uril mediated dimerization

T.D. Dang; H. Nguyen; M. Merkx; L. Brunsveld

doi:10.1002/anie.201208239

Supramolecular control of enzyme activity through cucurbit[8]uril mediated dimerization

T.D. Dang, H. Nguyen, M. Merkx, L. Brunsveld

Research output: Contribution to journal › Article › Academic › peer-review

106 Citations (Scopus)

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Abstract

At the double: Cucurbit[8]uril-mediated protein dimerization enables reversible control over strong enzyme activation of caspases. Simple addition of a short N-terminal FGG motif allows for a supramolecular-mediated 50-fold enhancement of caspase-9 catalytic activity.

Original language	English
Pages (from-to)	2915-2919
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	52
Issue number	10
DOIs	https://doi.org/10.1002/anie.201208239
Publication status	Published - 2013

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10.1002/anie.201208239

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title = "Supramolecular control of enzyme activity through cucurbit[8]uril mediated dimerization",

abstract = "At the double: Cucurbit[8]uril-mediated protein dimerization enables reversible control over strong enzyme activation of caspases. Simple addition of a short N-terminal FGG motif allows for a supramolecular-mediated 50-fold enhancement of caspase-9 catalytic activity.",

author = "T.D. Dang and H. Nguyen and M. Merkx and L. Brunsveld",

year = "2013",

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AU - Merkx, M.

AU - Brunsveld, L.

PY - 2013

Y1 - 2013

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AB - At the double: Cucurbit[8]uril-mediated protein dimerization enables reversible control over strong enzyme activation of caspases. Simple addition of a short N-terminal FGG motif allows for a supramolecular-mediated 50-fold enhancement of caspase-9 catalytic activity.

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DO - 10.1002/anie.201208239

M3 - Article

C2 - 23355250

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VL - 52

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 10

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Supramolecular control of enzyme activity through cucurbit[8]uril mediated dimerization

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