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• W3000284414 startingPage "1195" @default.
• W3000284414 abstract "A polyproline fragment containing a catalytic dyad of His–His or Ser–His was coupled with a self-assembling peptide MAX1 to design new hydrolases (H2H5 and H2S5) for catalyzing ester hydrolysis. Circular dichroism measurements indicated that the peptides change their conformation from random coils to β-sheets when pH increases from 5 to 10. IR spectra also displayed the vibration modes corresponding to their β-structures at pH 9.0. Transmission electron microscopy (TEM) and atomic force microscopy (AFM) measurements showed that in solution, the designed peptides self-assemble into network fibrils having a significantly increased catalytic efficiency on ester hydrolysis. On p-nitrophenyl acetate (p-NPA) substrate, the designed peptides exhibit high catalytic efficiency at pH 9.0 (kcat/KM = 12.1 M–1 s–1 for H2H5, 13.3 M–1 s–1 for H2S5), and their efficiency is even better at pH 10.0 (kcat/KM = 24.3 M–1 s–1 for H2H5, 99.4 M–1 s–1 for H2S5). Additionally, H2H5 and H2S5 also display good activity on catalyzing the hydrolysis of p-nitrophenyl-(2-phenyl)-propanoate (p-NPP) and p-nitrophenyl methoxyacetate (p-NPMA). Combining the polyproline-based catalytic scaffold with a self-assembling peptide generates an efficient hydrolase, providing a new design for effective artificial enzymes." @default.
• W3000284414 created "2020-01-23" @default.
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• W3000284414 date "2020-01-17" @default.
• W3000284414 modified "2023-10-14" @default.
• W3000284414 title "Conjugating Catalytic Polyproline Fragments with a Self-Assembling Peptide Produces Efficient Artificial Hydrolases" @default.
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• W3000284414 doi "https://doi.org/10.1021/acs.biomac.9b01620" @default.
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