Abstract
Antibody-based molecular recognition plays a central role in today's life sciences, ranging from immunoassays to molecular imaging and antibody-based therapeutics. Control over antibody activity by using external triggers such as light could further increase the specificity of antibody-based targeting. Here we present bivalent peptide–DNA ligands containing photocleavable linkers as a noncovalent approach by which to allow photoactivation of antibody activity. Light-triggered cleavage of the 3-amino-3-(2-nitrophenyl)propionic acid peptide linker converted the high-affinity bivalent peptide–DNA lock into weakly binding monovalent ligands, effectively restoring antibody targeting of cell-surface receptors. In this work, a proof of principle was provided with an anti-hemagglutinin antibody, but the molecular design of the lock is generic and applicable to any monoclonal antibody for which an epitope or mimotope of sufficient affinity is available.
Original language | English |
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Pages (from-to) | 2463-2466 |
Number of pages | 4 |
Journal | ChemBioChem |
Volume | 20 |
Issue number | 19 |
DOIs | |
Publication status | Published - 1 Oct 2019 |
Event | 1st International Workshop on Metals in Medicine: Chimie ParisTech - Paris, France Duration: 14 Nov 2019 → 15 Nov 2019 |
Keywords
- antibodies
- bivalent ligands
- caged ligands
- optogenetics
- photolysis