Premium
On‐Chip Neo‐Glycopeptide Synthesis for Multivalent Glycan Presentation
Author(s) -
Mende Marco,
Tsouka Alexandra,
Heidepriem Jasmin,
Paris Grigori,
Mattes Daniela S.,
Eickelmann Stephan,
Bordoni Vittorio,
Wawrzinek Robert,
Fuchsberger Felix F.,
Seeberger Peter H.,
Rademacher Christoph,
Delbianco Martina,
Mallagaray Alvaro,
Loeffler Felix F.
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202001291
Subject(s) - glycan , chemistry , glycome , click chemistry , concanavalin a , avidity , glycopeptide , nanotechnology , biophysics , combinatorial chemistry , biochemistry , glycoprotein , materials science , biology , in vitro , immunology , antibody , antibiotics
Single glycan–protein interactions are often weak, such that glycan binding partners commonly utilize multiple, spatially defined binding sites to enhance binding avidity and specificity. Current array technologies usually neglect defined multivalent display. Laser‐based array synthesis technology allows for flexible and rapid on‐surface synthesis of different peptides. By combining this technique with click chemistry, neo‐glycopeptides were produced directly on a functionalized glass slide in the microarray format. Density and spatial distribution of carbohydrates can be tuned, resulting in well‐defined glycan structures for multivalent display. The two lectins concanavalin A and langerin were probed with different glycans on multivalent scaffolds, revealing strong spacing‐, density‐, and ligand‐dependent binding. In addition, we could also measure the surface dissociation constant. This approach allows for a rapid generation, screening, and optimization of a multitude of multivalent scaffolds for glycan binding.