File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Peptide-induced super-assembly of biocatalytic metal-organic frameworks for programmed enzyme cascades

TitlePeptide-induced super-assembly of biocatalytic metal-organic frameworks for programmed enzyme cascades
Authors
KeywordsCatalyst activity
Crystalline materials
Organometallics
Peptides
Activity enhancement
Issue Date2019
PublisherRoyal Society of Chemistry: Open Access. The Journal's web site is located at http://www.rsc.org/publishing/journals/sc/About.asp
Citation
Chemical Science, 2019, v. 10 n. 34, p. 7852-7858 How to Cite?
AbstractDespite the promise of metal-organic frameworks (MOFs) as functional matrices for enzyme stabilization, the development of a stimulus-responsive approach to induce multi-enzyme cascade reaction in MOFs remains a critical challenge. Here, a novel method using peptide-induced super-assembly of MOFs is developed for programmed enzyme cascade reactions on demand. The super-assembled MOF particles containing different enzymes shows remarkable 7.3-fold and 4.4-fold catalytic activity enhancements for the two-enzyme and three-enzyme cascade reactions, respectively, as compared with the unassembled MOF nanoparticles. Further digestion of the coiled-coil forming peptides on the MOF surfaces lead to the MOFs superstructure disassembly and the programmed enzyme cascade reaction to be “switched-off”. Research on these stimuli-responsive materials with controllable and predictable biocatalytic functions/properties provide a concept to facilitate the fabrication of next-generation smart materials based on precision chemistry.
Descriptioneid_2-s2.0-85072053044
Persistent Identifierhttp://hdl.handle.net/10722/284484
ISSN
2023 Impact Factor: 7.6
2023 SCImago Journal Rankings: 2.333
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLiang, J-
dc.contributor.authorMazur, F-
dc.contributor.authorTang, C-
dc.contributor.authorNing, X-
dc.contributor.authorChandrawati, R-
dc.contributor.authorLiang, K-
dc.date.accessioned2020-08-07T08:58:18Z-
dc.date.available2020-08-07T08:58:18Z-
dc.date.issued2019-
dc.identifier.citationChemical Science, 2019, v. 10 n. 34, p. 7852-7858-
dc.identifier.issn2041-6520-
dc.identifier.urihttp://hdl.handle.net/10722/284484-
dc.descriptioneid_2-s2.0-85072053044-
dc.description.abstractDespite the promise of metal-organic frameworks (MOFs) as functional matrices for enzyme stabilization, the development of a stimulus-responsive approach to induce multi-enzyme cascade reaction in MOFs remains a critical challenge. Here, a novel method using peptide-induced super-assembly of MOFs is developed for programmed enzyme cascade reactions on demand. The super-assembled MOF particles containing different enzymes shows remarkable 7.3-fold and 4.4-fold catalytic activity enhancements for the two-enzyme and three-enzyme cascade reactions, respectively, as compared with the unassembled MOF nanoparticles. Further digestion of the coiled-coil forming peptides on the MOF surfaces lead to the MOFs superstructure disassembly and the programmed enzyme cascade reaction to be “switched-off”. Research on these stimuli-responsive materials with controllable and predictable biocatalytic functions/properties provide a concept to facilitate the fabrication of next-generation smart materials based on precision chemistry.-
dc.languageeng-
dc.publisherRoyal Society of Chemistry: Open Access. The Journal's web site is located at http://www.rsc.org/publishing/journals/sc/About.asp-
dc.relation.ispartofChemical Science-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectCatalyst activity-
dc.subjectCrystalline materials-
dc.subjectOrganometallics-
dc.subjectPeptides-
dc.subjectActivity enhancement-
dc.titlePeptide-induced super-assembly of biocatalytic metal-organic frameworks for programmed enzyme cascades-
dc.typeArticle-
dc.identifier.emailTang, C: tangc@hku.hk-
dc.identifier.authorityTang, C=rp01765-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1039/C9SC02021G-
dc.identifier.scopuseid_2-s2.0-85072053044-
dc.identifier.hkuros312226-
dc.identifier.volume10-
dc.identifier.issue34-
dc.identifier.spage7852-
dc.identifier.epage7858-
dc.identifier.isiWOS:000482978700024-
dc.publisher.placeUnited Kingdom-
dc.identifier.issnl2041-6520-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats