Allosterically Regulated Phosphatase Activity from Peptide–PNA Conjugates Folded Through Hybridization. Issue 30 (20th June 2016)

• Record Type: Journal Article
• Authors: Machida, Takuya; Dutt, Som; Winssinger, Nicolas
• Is Part Of: Angewandte Chemie international edition. Volume 55:Issue 30(2016)
• Page Start: 8595
• Page End: 8598
• Publication Date: 2016-06-20
• Subjects: catalysis -- peptides -- PNA -- system chemistry; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201602751
• Languages: English
• ISSNs: 1433-7851

Abstract

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. Abstract : A library of peptides that are constrained in a hairpin loop by flanking peptide nucleic acids upon hybridization were synthesized. A screen for phosphatase activity led to the discovery of a catalyst with a more than 25‐fold rate acceleration over the linear peptide. The hybridization‐enforced folding of the peptide is decisive for the activity.