Enzyme Conformation Influences the Performance of Lipase-powered Nanomotors
dc.contributor.author
dc.date.accessioned
2023-07-17T06:17:37Z
dc.date.available
2023-07-17T06:17:37Z
dc.date.issued
2020-11-16
dc.identifier.issn
1433-7851
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dc.description.abstract
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 mm). 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
dc.description.sponsorship
L. W. thanks the NSFC (No. 51703043), the Marie Sklodowska-Curie Fellowship (Grant No. 712754), and the Severo Ochoa programme (Grant SEV-2014-0425(2015-2019)). X.H. appreciates the NSFC (No. 21871069). P.E.D.S.R acknowledges postdoctoral fellowship support from the Spanish MINECO “Juan de la Cierva formación” program 2016 FJCI-2016-29512. M.M, Y.L.M. and M.F. are grateful to the Comunidad Autonoma de Madrid and FEDER for the I+D collaborative Programme in Biomedicine NIETO-CM (Project reference B2017-BMD3731). S.O. thanks the Generalitat de Catalunya for the emerging group CompBioLab (No. 2017 SGR-1707), Spanish MINECO for project PGC2018-102192-B-I00, and the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program (No. ERC-2015-StG-679001). J.I.F. acknowledges postdoctoral fellowship support from the Spanish MINECO “Juan de la Cierva formación” program IJCI-2017-34129, and the Marie Sklodowska-Curie Fellowship (H2020-MSCA-IF-2016-753045, J.I.F). M.F. thanks MINECO for the research grant No. SAF2014-59118-JIN co-funded by FEDER and also the Comunidad Autonoma de Madrid for research project No. 2017-T1/BIO-4992 (“Atracción de Talento” Action) co-funded by Universidad Complutense de Madrid. The CNIC is supported by MINECO and the Pro-CNIC Foundation and is a Severo Ochoa Centre of Excellence (SEV-2015-0505). S.S. thanks the Spanish MINECO for grants CTQ2015-68879-R (MICRODIA) and CTQ2015-72741-EXP (Enzwim), and Proyecto RTI2018-098164-B-I00 funded by MCIU/AEI/FEDER, UE
dc.format.mimetype
application/pdf
dc.language.iso
eng
dc.publisher
Wiley
dc.relation
PGC2018-102192-B-I00
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Versió postprint del document publicat a: https://doi.org/10.1002/anie.202008339
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© Angewandte Chemie: iInternational Eedition, 2020, vol. 59, núm. 47, p. 21080-21087
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Articles publicats (D-Q)
dc.rights
Tots els drets reservats
dc.subject
dc.title
Enzyme Conformation Influences the Performance of Lipase-powered Nanomotors
dc.type
info:eu-repo/semantics/article
dc.rights.accessRights
info:eu-repo/semantics/openAccess
dc.relation.projectID
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-102192-B-I00/ES/EVOLUCION COMPUTACIONAL DE ENZIMAS MEDIANTE LA EXPLORACION DE LA SUPERFICIE CONFORMACIONAL/
info:eu-repo/grantAgreement/EC/H2020/679001/EU/Network models for the computational design of proficient enzymes/NetMoDEzyme
dc.type.version
info:eu-repo/semantics/acceptedVersion
dc.identifier.doi
dc.identifier.idgrec
031790
dc.contributor.funder
dc.type.peerreviewed
peer-reviewed
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dc.relation.ProjectAcronym
dc.identifier.eissn
1521-3773