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Optical Control of Antibody Activity by Using Photocleavable Bivalent Peptide-DNA Locks.

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.

SUBMITTER: Wouters SFA

PROVIDER: S-EPMC6790702 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

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Optical Control of Antibody Activity by Using Photocleavable Bivalent Peptide-DNA Locks.

Wouters Simone F A SFA Wijker Elvira E Merkx Maarten M

Chembiochem : a European journal of chemical biology 20190903 19

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-a ...[more]

PMID: 31074548

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