Switchable Hydrolase Based on Reversible Formation of Supramolecular Catalytic Site Using a Self‐Assembling Peptide
Abstract
The reversible regulation of catalytic activity is a feature found in natural enzymes which is not commonly observed in artificial catalytic systems. Here, we fabricate an artificial hydrolase with pH‐switchable activity, achieved by introducing a catalytic histidine residue at the terminus of a pH‐responsive peptide. The peptide exhibits a conformational transition from random coil to β‐sheet by changing the pH from acidic to alkaline. The β‐sheet self‐assembles to form long fibrils with the hydrophobic edge and histidine residues extending in an ordered array as the catalytic microenvironment, which shows significant esterase activity. Catalytic activity can be reversible switched by pH‐induced assembly/disassembly of the fibrils into random coils. At higher concentrations, the peptide forms a hydrogel which is also catalytically active and maintains its reversible (de‐)activation.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Oct 11, 2017
- Source ID
- 10.1002/ange.201708036
Entities
People
- Ayala Lampel
- Charalampos G Pappas
- Charles Maldarelli
- Chunqiu Zhang
- Douglas MacPherson
- Ramim Shafi
- Rein V Ulijn
- Tong Wang
- Vishal Narang
Organizations
- CUNY Graduate School and University Center
- City University of New York
- Hunter College
- National Science Foundation