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

Article Article scientifique Article Allosterically Regulated Phosphatase Activity from Peptide-PNA Conjugates Folded Through Hybridization eng 2016 author Machida Takuya 806195 author Dutt Som 811570 author Winssinger Nicolas 769664 8595-8598 10.1002/anie.201602751 1433-7851 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. Dewey 540 36 Département de chimie organique 141 false 762 Groupe Winssinger Angewandte Chemie 55 30 deadae56-b519-4692-ba71-6fb8fddebbff Article (Published version) Restricted Machida_et_al-2016-Angewandte_Chemie_International_Edition.pdf 2775618 application/pdf restrictedAccess Faculté des sciences / Section de chimie et biochimie / Département de chimie organique

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Allosterically Regulated Phosphatase Activity from Peptide-PNA Conjugates Folded Through Hybridization	Angewandte Chemie			2016	618	9

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