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 |
|---|---|
| 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 |
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Keywords
- antibodies
- bivalent ligands
- caged ligands
- optogenetics
- photolysis
Cite this
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Optical control of antibody activity using photocleavable bivalent peptide-DNA locks. / Wouters, Simone; Wijker, E.; Merkx, Maarten (Corresponding author).
In: ChemBioChem, Vol. 20, No. 19, 01.10.2019, p. 2463-2466.Research output: Contribution to journal › Article › Academic › peer-review
TY - JOUR
T1 - Optical control of antibody activity using photocleavable bivalent peptide-DNA locks
AU - Wouters, Simone
AU - Wijker, E.
AU - Merkx, Maarten
PY - 2019/10/1
Y1 - 2019/10/1
N2 - 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.
AB - 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.
KW - antibodies
KW - bivalent ligands
KW - caged ligands
KW - optogenetics
KW - photolysis
UR - http://www.scopus.com/inward/record.url?scp=85071644648&partnerID=8YFLogxK
U2 - 10.1002/cbic.201900241
DO - 10.1002/cbic.201900241
M3 - Article
C2 - 31074548
VL - 20
SP - 2463
EP - 2466
JO - ChemBioChem
JF - ChemBioChem
SN - 1439-4227
IS - 19
ER -