Intrinsic enzymatic properties modulate the self-propulsion of micromotors

Xavier Arqué, Adrian Romero-Rivera, Ferran Feixas, Tania Patiño (), Sílvia Osuna () and Samuel Sánchez ()
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Xavier Arqué: The Barcelona Institute of Science and Technology (BIST)
Adrian Romero-Rivera: Universitat de Girona
Ferran Feixas: Universitat de Girona
Tania Patiño: The Barcelona Institute of Science and Technology (BIST)
Sílvia Osuna: Universitat de Girona
Samuel Sánchez: The Barcelona Institute of Science and Technology (BIST)

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Bio-catalytic micro- and nanomotors self-propel by the enzymatic conversion of substrates into products. Despite the advances in the field, the fundamental aspects underlying enzyme-powered self-propulsion have rarely been studied. In this work, we select four enzymes (urease, acetylcholinesterase, glucose oxidase, and aldolase) to be attached on silica microcapsules and study how their turnover number and conformational dynamics affect the self-propulsion, combining both an experimental and molecular dynamics simulations approach. Urease and acetylcholinesterase, the enzymes with higher catalytic rates, are the only enzymes capable of producing active motion. Molecular dynamics simulations reveal that urease and acetylcholinesterase display the highest degree of flexibility near the active site, which could play a role on the catalytic process. We experimentally assess this hypothesis for urease micromotors through competitive inhibition (acetohydroxamic acid) and increasing enzyme rigidity (β-mercaptoethanol). We conclude that the conformational changes are a precondition of urease catalysis, which is essential to generate self-propulsion.

Date: 2019
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DOI: 10.1038/s41467-019-10726-8

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