Logo of Humboldt-Universität zu BerlinLogo of Humboldt-Universität zu Berlin
edoc-Server
Open-Access-Publikationsserver der Humboldt-Universität
de|en
Header image: facade of Humboldt-Universität zu Berlin
View Item 
  • edoc-Server Home
  • Artikel und Monographien
  • Zweitveröffentlichungen
  • View Item
  • edoc-Server Home
  • Artikel und Monographien
  • Zweitveröffentlichungen
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.
All of edoc-ServerCommunity & CollectionTitleAuthorSubjectThis CollectionTitleAuthorSubject
PublishLoginRegisterHelp
StatisticsView Usage Statistics
All of edoc-ServerCommunity & CollectionTitleAuthorSubjectThis CollectionTitleAuthorSubject
PublishLoginRegisterHelp
StatisticsView Usage Statistics
View Item 
  • edoc-Server Home
  • Artikel und Monographien
  • Zweitveröffentlichungen
  • View Item
  • edoc-Server Home
  • Artikel und Monographien
  • Zweitveröffentlichungen
  • View Item
2020-08-04Zeitschriftenartikel DOI: 10.18452/22169
Rational Design of a DNA-Scaffolded High-Affinity Binder for Langerin
Bachem, Gunnar
Wamhoff, Eike-Christian cc
Silberreis, Kim
Kim, Dongyoon cc
Baukmann, Hannes cc
Fuchsberger, Felix F. cc
Dernedde, Jens cc
Rademacher, Christoph cc
Seitz, Oliver cc
Fuchsberger, Felix
Mathematisch-Naturwissenschaftliche Fakultät
Binders of langerin could target vaccines to Langerhans cells for improved therapeutic effect. Since langerin has low affinity for monovalent glycan ligands, highly multivalent presentation has previously been key for targeting. Aiming to reduce the amount of ligand required, we rationally designed molecularly defined high‐affinity binders based on the precise display of glycomimetic ligands (Glc2NTs) on DNA‐PNA scaffolds. Rather than mimicking langerin's homotrimeric structure with a C3‐symmetric scaffold, we developed readily accessible, easy‐to‐design bivalent binders. The method considers the requirements for bridging sugar binding sites and statistical rebinding as a means to both strengthen the interactions at single binding sites and amplify the avidity enhancement provided by chelation. This gave a 1150‐fold net improvement over the affinity of the free ligand and provided a nanomolar binder (IC50=300 nM) for specific internalization by langerin‐expressing cells.
Files in this item
Thumbnail
anie.202006880.pdf — Adobe PDF — 1.230 Mb
MD5: 4f4f73a4081b0e58eaf612937c2066cf
Cite
BibTeX
EndNote
RIS
(CC BY 4.0) Attribution 4.0 International(CC BY 4.0) Attribution 4.0 International
Details
DINI-Zertifikat 2019OpenAIRE validatedORCID Consortium
Imprint Policy Contact Data Privacy Statement
A service of University Library and Computer and Media Service
© Humboldt-Universität zu Berlin
 
DOI
10.18452/22169
Permanent URL
https://doi.org/10.18452/22169
HTML
<a href="https://doi.org/10.18452/22169">https://doi.org/10.18452/22169</a>