dc.contributor.author
Mikolajczak, Dorian J.
dc.contributor.author
Berger, Allison Ann
dc.contributor.author
Koksch, Beate
dc.date.accessioned
2020-05-26T12:57:42Z
dc.date.available
2020-05-26T12:57:42Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/27543
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-27298
dc.description.abstract
The self‐assembly of peptides onto the surface of gold nanoparticles has emerged as a promising strategy towards the creation of artificial enzymes. The resulting high local peptide density surrounding the nanoparticle leads to cooperative and synergistic effects, which result in rate accelerations and distinct catalytic properties compared to the unconjugated peptide. This Minireview summarizes contributions to and progress made in the field of catalytically active peptide–gold nanoparticle conjugates. The origin of distinct properties, as well as potential applications, are also discussed.
en
dc.format.extent
10 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
artificial enzymes
en
dc.subject
gold nanoparticles
en
dc.subject
self-assembly
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::540 Chemie::547 Organische Chemie
dc.title
Catalytically active peptide–gold nanoparticle conjugates: Prospecting for artificial enzymes
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.doi
10.1002/anie.201908625
dcterms.bibliographicCitation.journaltitle
Angewandte Chemie
dcterms.bibliographicCitation.number
23
dcterms.bibliographicCitation.pagestart
8776
dcterms.bibliographicCitation.pageend
8785
dcterms.bibliographicCitation.volume
59
dcterms.bibliographicCitation.url
https://doi.org/10.1002/anie.201908625
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.affiliation.other
Institut für Chemie und Biochemie / Organische Chemie
refubium.funding
DEAL Wiley
refubium.note.author
Die Publikation wurde von der Freien Universität Berlin finanziert.
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
1521-3773