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Enzyme Conformation Influences the Performance of Lipase‐powered Nanomotors
Author(s) -
Wang Lei,
Marciello Marzia,
EstévezGay Miquel,
Soto Rodriguez Paul E. D.,
Luengo Morato Yurena,
IglesiasFernández Javier,
Huang Xin,
Osuna Sílvia,
Filice Marco,
Sánchez Samuel
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.202008339
Subject(s) - triacetin , lipase , enzyme , molecular dynamics , chemistry , catalysis , nanotechnology , biophysics , materials science , combinatorial chemistry , organic chemistry , computational chemistry , biology
Enzyme‐powered micro/nanomotors have myriads of potential applications in various areas. To efficiently reach those applications, it is necessary and critical to understand the fundamental aspects affecting the motion dynamics. Herein, we explored the impact of enzyme orientation on the performance of lipase‐powered nanomotors by tuning the lipase immobilization strategies. The influence of the lipase orientation and lid conformation on substrate binding and catalysis was analyzed using molecular dynamics simulations. Besides, the motion performance indicates that the hydrophobic binding (via OTES) represents the best orienting strategy, providing 48.4 % and 95.4 % increase in diffusion coefficient compared to hydrophilic binding (via APTES) and Brownian motion (no fuel), respectively (with C [triacetin] of 100 m m ). This work provides vital evidence for the importance of immobilization strategy and corresponding enzyme orientation for the catalytic activity and in turn, the motion performance of nanomotors, and is thus helpful to future applications.

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