Switchable Hydrolase Based on Reversible Formation of Supramolecular Catalytic Site Using a Self-Assembling Peptide

Chunqiu Zhang, Ramim Shafi, Ayala Lampel, Douglas MacPherson, Charalampos G. Pappas, Vishal Narang, Tong Wang, Charles Maldarelli*, Rein V. Ulijn

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)14511-14515
Number of pages5
JournalAngewandte Chemie - International Edition
Volume56
Issue number46
DOIs
StatePublished - 13 Nov 2017
Externally publishedYes

Funding

FundersFunder number
CUNY ASRC
NSF-CBET
U.S. Army Research OfficeW911NF-16-1-0113
National Science Foundation1512458
Army Research Laboratory

    Keywords

    • artificial hydrolase
    • pH-switch
    • peptide
    • self-assembly

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