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Allosterically Regulated Phosphatase Activity from Peptide-PNA Conjugates Folded Through Hybridization

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Published in Angewandte Chemie: International Edition. 2016, vol. 55, no. 30, p. 8595-8598
Abstract The importance of spatial organization in short peptide catalysts is well recognized. We synthesized and screened a library of peptides flanked by peptide nucleic acids (PNAs) such that the peptide would be constrained in a hairpin loop upon hybridization. A screen for phosphatase activity led to the discovery of a catalyst with >25-fold rate acceleration over the linear peptide. We demonstrated that the hybridization-enforced folding of the peptide is necessary for activity, and designed a catalyst that is allosterically controlled using a complementary PNA sequence.
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Other version: http://doi.wiley.com/10.1002/anie.201602751
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Research group Groupe Winssinger
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MACHIDA, Takuya, DUTT, Som, WINSSINGER, Nicolas. Allosterically Regulated Phosphatase Activity from Peptide-PNA Conjugates Folded Through Hybridization. In: Angewandte Chemie: International Edition, 2016, vol. 55, n° 30, p. 8595-8598. https://archive-ouverte.unige.ch/unige:85392

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Deposited on : 2016-07-20

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