dc.contributor.author
Exner, Matthias P.
dc.contributor.author
Köhling, Sebastian
dc.contributor.author
Rivollier, Julie
dc.contributor.author
Gosling, Sandrine
dc.contributor.author
Srivastava, Puneet
dc.contributor.author
Palyancheva, Zheni I.
dc.contributor.author
Herdewijn, Piet
dc.contributor.author
Heck, Marie-Pierre
dc.contributor.author
Rademann, Jörg
dc.contributor.author
Budisa, Nediljko
dc.date.accessioned
2018-06-08T03:55:45Z
dc.date.available
2016-06-24T10:18:28.007Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/16236
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-20420
dc.description.abstract
The increasing need for site-specific protein decorations that mimic natural
posttranslational modifications requires access to a variety of noncanonical
amino acids with moieties enabling bioorthogonal conjugation chemistry. Here
we present the incorporation of long-chain olefinic amino acids into model
proteins with rational variants of pyrrolysyl-tRNA synthetase (PylRS). Nε-
heptenoyl lysine was incorporated for the first time using the known
promiscuous variant PylRS(Y306A/Y384F), and Nε-pentenoyl lysine was
incorporated in significant yields with the novel variant PylRS(C348A/Y384F).
This is the only example of rational modification at position C348 to enlarge
the enzyme’s binding pocket. Furthermore, we demonstrate the feasibility of
our chosen amino acids in the thiol-ene conjugation reaction with a thiolated
polysaccharide.
en
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
stop codon suppression
dc.subject
protein decoration
dc.subject
noncanonical amino acid
dc.subject
pyrrolysyl-tRNA synthetase
dc.subject
thiol-ene coupling
dc.subject.ddc
500 Naturwissenschaften und Mathematik::540 Chemie
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie
dc.title
Incorporation of Amino Acids with Long-Chain Terminal Olefins into Proteins
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Molecules. - 21 (2016), 3, Artikel Nr. 287
dcterms.bibliographicCitation.doi
10.3390/molecules21030287
dcterms.bibliographicCitation.url
http://dx.doi.org/10.3390/molecules21030287
refubium.affiliation
Biologie, Chemie, Pharmazie
de
refubium.mycore.fudocsId
FUDOCS_document_000000024891
refubium.note.author
Der Artikel wurde in einer Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000006683
dcterms.accessRights.openaire
open access