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2020-01-07Zeitschriftenartikel DOI: 10.18452/21067
Mussel-Inspired Polymerization of Peptides
dc.contributor.authorKohn, Jana M.
dc.contributor.authorRiedel, Jerome
dc.contributor.authorHorsch, Justus
dc.contributor.authorStephanowitz, Heike
dc.contributor.authorBörner, Hans G.
dc.date.accessioned2020-01-22T09:23:15Z
dc.date.available2020-01-22T09:23:15Z
dc.date.issued2020-01-07none
dc.identifier.other10.1002/marc.201900431
dc.identifier.urihttp://edoc.hu-berlin.de/18452/21815
dc.description.abstractA previously introduced tyrosinase‐activated polymerization of Tyr‐ and Cys‐bearing peptides yielding artificial mussel‐glue proteins is realized without the need of the specific enzyme by a chemical activation route. This decouples the sequence of polymerizable peptides (unimers) from the constraints of tyrosinase substrates and enables the polymerization of minimal motifs such as Dopa‐Lys‐Cys (Umini*KC) or Dopa‐Gly‐Cys (Umini*GC). In the polymerization procedure, sodium periodate is used to oxidize Dopa residues of the unimers to Dopa‐quinones to which the thiol of a Cys residue is added in a Michael‐type reaction. The resulting polyUmini*KC and polyUmini*GC exhibit a thiol–catechol connectivity as a potent adhesive functionality at each repeat unit. QCM‐D experiments show the excellent substrate adsorption properties of the products from the chemically activated polymerization. On aluminum oxide surfaces, polyUmini*KC rapidly forms a coating, even under seawater model conditions and the coating resists rinsing with hypersaline solution of 4.2 M salt mixtures. While the sodium periodate oxidation is less specific than the tyrosinase reaction and requires the implementation of Dopa instead of Tyr residues into the polymerizable unimers, the chemical route makes scale‐up more easily accessible.eng
dc.language.isoengnone
dc.publisherHumboldt-Universität zu Berlin
dc.rights(CC BY 4.0) Attribution 4.0 Internationalger
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftennone
dc.titleMussel-Inspired Polymerization of Peptidesnone
dc.typearticle
dc.subtitleThe Chemical Activation Route as Key to Broaden the Sequential Space of Artificial Mussel-Glue Proteinsnone
dc.identifier.urnurn:nbn:de:kobv:11-110-18452/21815-5
dc.identifier.doihttp://dx.doi.org/10.18452/21067
dc.type.versionpublishedVersionnone
local.edoc.container-titleMacromolecular rapid communicationsnone
local.edoc.pages7none
local.edoc.type-nameZeitschriftenartikel
local.edoc.institutionMathematisch-Naturwissenschaftliche Fakultätnone
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-publisher-nameWiley-VCHnone
local.edoc.container-publisher-placeWeinheimnone
local.edoc.container-volume41none
local.edoc.container-issue1none
dc.description.versionPeer Reviewednone
local.edoc.container-articlenumber1900431none
dc.identifier.eissn1521-3927

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