Chemo-Enzymatic Site-Specific Photocaging of Peptides and Proteins

INV-17072

 

Photocaging is a process in which a molecule is covalently modified by a photolabile group; the molecule is often referred to as being ‘caged.’ Typically. caging renders the molecule non-functional. Subsequently, photolysis of such ‘caged’ peptides and proteins removes the photolabile group and regenerates the native (or unmodified) peptides and proteins, thereby unmasking the original activity. In essence, the caging and decaging permits both temporal and spatial control of peptide and protein function.

Photocaging has broad applications in chemistry, biology, medicine, materials sciences, and other fields; however, past photocaging techniques have typically employed chemical methods which are limited to small and simple peptides, and are not site-specific.

 

The proposed technology is a novel site‑specific photocaging technique that utilizes the properties of peptides and proteins, which modulate numerous biological functions via interactions with their respective target. 

Transglutaminase enzymes catalyze an acyl group transfer reaction in which glutamine substrates act as acyl donors and various nucleophiles act as acyl acceptors. As each transglutaminase isoform has unique substrate specificity requirements, this provides an excellent platform for site-specific conjugation applications. 

 

- Can be used to photocage large, complicated proteins and peptides 

- Highly tunable photocaging is possible

- Photocaging moiety can be further derivatized with orthogonal chemistry to generate photocaged conjugates 

 

- Controlled release of protein therapeutics

- Bioconjugation 

- Light-controlled delivery of photocaged conjugates 

- Biological probes

- Cell/protein adhesion to surfaces

- Materials sciences

 

- License

- Partnering

- Research collaboration