caged peptide have covalently attached groups that are rapidly cleaved upon exposure to UV light - peptide-bonds-are-formed-by-hydrolysis have covalently attached groups that are rapidly cleaved upon exposure to UV light Unlocking Biological Control: The Power of Caged Peptides

calcitonin-gene-related-peptide-cgrp-a-new-target-for-migraine Caged peptides represent a sophisticated class of biomolecules engineered for precise temporal and spatial control over biological processes作者：J Dai·2022·被引用次数：68—In tumor cells, acaged peptide-AIEgen probe self-assembled with miR-140 could release the GO203 peptide binding to MUC1 and miR-140 .... By temporarily masking a peptide's activity with a photolabile protecting group, researchers can achieve targeted activation, often utilizing light as the trigger. This innovative approach has opened new avenues in fields ranging from neuroscience to biomaterials and drug deliveryCaged chemotactic peptides - PubMed - NIH.

The fundamental principle behind caged compounds, including caged peptides, is the covalent attachment of a group that renders the molecule inactive.Caged Compounds: Small Molecules and Peptides This group is designed to be rapidly cleaved upon exposure to specific wavelengths of light, typically ultraviolet (UV) light. This "uncaging" process releases the active peptide, allowing for the initiation of its intended biological function. This ability to precisely control the release of active agents is crucial for studying fast biological events and for developing advanced therapeutic strategies.

The synthesis of caged peptides involves attaching these photo-protecting groups (PPGs) to specific sites on the peptide, such as the side chains of amino acids or the termini. The choice of protecting group and its attachment site is critical for ensuring efficient uncaging and maintaining the peptide's biological integrity. For instance, research has explored the solid-phase synthesis of caged peptides that incorporate photolabile derivatives of amino acids like aspartic acid. In some applications, backbone-caged peptides are synthesized, offering diverse sites for introducing photocleavable groups, contrasting with side-chain modifications.

The applications of caged peptides are remarkably diverse.Synthesis and application of caged peptides and proteins In neuroscience, caged peptides targeted against calmodulin have been instrumental in investigating the rapid roles of calcium-calmodulin and myosin II in cellular motilitySignaling pathways underlying eosinophil cell motility .... Similarly, extracellular caged peptide inhibitors of AMPA subtype of glutamate receptor have been employed to differentiate between fast single-site transmission and slower, multi-synapse signaling. This precise control over neurotransmitter release or inhibition allows for a deeper understanding of neural circuit function作者：D Humphrey·2007·被引用次数：2—A caged compound, peptide, or protein isprepared by covalently linking it to a photolabile, protecting group via a limited number of critical functional groups ....

Beyond neuronal signaling, caged peptides are revolutionizing biomaterials作者：Y Tatsu—'Solid-phase synthesis of caged peptidescontaining photolabile derivatives of aspartic acid' published in 'Peptides Frontiers of Peptide Science'. The development of photoinduced hydrogel-forming caged peptides, such as the caged-EAK16-II peptide, allows for the practical production of self-assembling peptide hydrogels. Upon light exposure, the caged peptide undergoes uncaging and structural transition, leading to hydrogel formation. This technology holds promise for tissue engineering and regenerative medicine, enabling the controlled formation of scaffolds for cell growth and differentiation. Another advancement is the design of a photo-caged peptide that transitions from an antifouling ligand to a cell-binding ligand upon light activation, facilitating controlled cell adhesion to biomaterial surfaces.

Furthermore, caged peptides are being explored for targeted therapeutic interventions. A caged antimicrobial peptide integrated into liposomes has been developed as a photocontrolled compound release system. This approach allows for the localized release of the antimicrobial agent only at the desired site, minimizing off-target effects. In cancer research, caged peptide probes have been designed to deliver therapeutic payloads, such as in the case of a caged peptide-AIEgen probe that, upon activation, releases a peptide targeting specific cancer cell markers. This strategy aims to achieve deep downregulation of proteins like PD-L1 in tumor cells.

The ability to control peptide activity with light has also extended to other biomolecules. For example, nucleobase-caged peptide nucleic acids (PNAs) have been synthesized, offering new possibilities for gene regulation and diagnosticsPhoto-caged peptides arepeptides that contain photo-protecting groups (PPGs) at the side-chain or termini, which can temporarily mask the original ....

The field of caged compounds is continuously evolving, with ongoing research focusing on improving the efficiency of uncaging, developing new protecting groups with different spectral sensitivities, and expanding the range of peptides that can be caged. The synthesis and application of caged peptides and proteins continue to be a vibrant area of research, promising further breakthroughs in understanding fundamental biological processes and developing innovative therapeutic and diagnostic tools. The ability to precisely manipulate biological activity using caged peptides underscores their importance as powerful tools in modern biological and biomedical research.