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Hydrostatic Pressure Increases the Catalytic Activity of Amyloid Fibril Enzymes
Author(s) -
Luong Trung Quan,
Erwin Nelli,
Neumann Matthias,
Schmidt Andreas,
Loos Cornelia,
Schmidt Volker,
Fändrich Marcus,
Winter Roland
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201605715
Subject(s) - hydrostatic pressure , activation energy , chemistry , catalysis , fibril , enzyme , esterase , volume (thermodynamics) , biophysics , amyloid fibril , absorption (acoustics) , amyloid β , materials science , biochemistry , thermodynamics , medicine , physics , disease , pathology , biology , composite material
We studied the combined effects of pressure (0.1–200 MPa) and temperature (22, 30, and 38 °C) on the catalytic activity of designed amyloid fibrils using a high‐pressure stopped‐flow system with rapid UV/Vis absorption detection. Complementary FT‐IR spectroscopic data revealed a remarkably high pressure and temperature stability of the fibrillar systems. High pressure enhances the esterase activity as a consequence of a negative activation volume at all temperatures (about −14 cm 3 mol −1 ). The enhancement is sustained in the whole temperature range covered, which allows a further acceleration of the enzymatic activity at high temperatures (activation energy 45–60 kJ mol −1 ). Our data reveal the great potential of using both pressure and temperature modulation to optimize the enzyme efficiency of catalytic amyloid fibrils.