dc.contributor.author
Perera-Bobusch, Chrischani
dc.contributor.author
Hormann, Jan
dc.contributor.author
Weise, Christoph
dc.contributor.author
Wedepohl, Stefanie
dc.contributor.author
Dernedde, Jens
dc.contributor.author
Kulak, Nora
dc.date.accessioned
2018-06-08T07:16:09Z
dc.date.available
2016-08-08T09:01:47.863Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/17538
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-21422
dc.description.abstract
A simple approach towards efficient artificial proteases based on the cyclen
ligand is presented. We thus achieved an increase of the proteolytic activity
of two orders of magnitude when compared to the unsubstituted cyclen complex.
Amphiphilic Cu(II) and Co(III) complexes cut BSA and myoglobin as model
substrates at μM concentrations. MALDI-ToF MS is used to identify the cleavage
fragments.
en
dc.rights.uri
http://creativecommons.org/licenses/by/3.0/
dc.subject.ddc
500 Naturwissenschaften und Mathematik::540 Chemie
dc.title
Significantly enhanced proteolytic activity of cyclen complexes by
monoalkylation
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Dalton Transactions. - 45 (2016), 26, S. 10500-10504
dcterms.bibliographicCitation.doi
10.1039/C6DT00681G
dcterms.bibliographicCitation.url
http://pubs.rsc.org/en/content/articlelanding/2016/dt/c6dt00681g#!divAbstract
refubium.affiliation
Biologie, Chemie, Pharmazie
de
refubium.funding
OpenAccess Publikation in Allianzlizenz
refubium.funding.id
Au-028837
refubium.mycore.fudocsId
FUDOCS_document_000000025056
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000006799
dcterms.accessRights.openaire
open access
