Switchable Hydrolase Based on Reversible Formation of Supramolecular Catalytic Site Using a Self-Assembling Peptide
| Autor: | Charles Maldarelli, Charalampos G. Pappas, V. Narang, Chunqiu Zhang, Ayala Lampel, Douglas S MacPherson, Rein V. Ulijn, Tong Wang, Ramim Shafi |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Circular dichroism
Spectrometry Mass Electrospray Ionization Stereochemistry Hydrolases Protein Conformation Supramolecular chemistry Peptide 02 engineering and technology 010402 general chemistry 01 natural sciences Catalysis Protein structure Catalytic Domain Hydrolase Histidine chemistry.chemical_classification Binding Sites 010405 organic chemistry Chemistry Circular Dichroism Hydrogels General Medicine General Chemistry Hydrogen-Ion Concentration 021001 nanoscience & nanotechnology Random coil 0104 chemical sciences Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization 0210 nano-technology Peptides Hydrophobic and Hydrophilic Interactions Self-assembling peptide |
| Zdroj: | Angewandte Chemie (International ed. in English). 56(46) |
| ISSN: | 1521-3773 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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