The photocleavable molecules using the chemically stable remote silyl group exhibited ideal molecular properties for chemical biology research and cellular experiments. We further utilized our developed photocleavable structure to create biomaterials enabling an efficient protein release. To achieve the desired molecular functionality for protein-releasing materials, we designed string-like photocleavable molecules termed photolinkers, with one end designed to bind to the protein of interest and the other end designed to bind to the solid phase material (Figure ). To connect proteins with photolinkers, we selected the HaloTag conjugation technology and installed a HaloTag binding ligand, hexyl chloride, on one end of the photolinkers. For binding to the solid phase material, the other end was designed to incorporate an azide group, allowing custom structural modifications suitable for diverse targets using click chemistry (Figure ). We prepared three types of photolinkers by stepwise chemical synthesis (Figure , Supplementary Scheme S2), namely non-decorated ester-linked coumarin (Esterphotolinker 7), non-decorated carbamate-linked coumarin (Carbphotolinker 8), and silyl-substituted carbamate-linked coumarin (Si-Carb-photolinker 9), to investigate and compare the effects of the remote silyl group. HaloTag-fused proteins were tethered to a magnetic beads using the synthesized photolinkers (Figure , Supplementary Scheme S3). Initially, we reacted an excess of photolinkers with commercially available biotin-BCN to quantitatively obtain the click product. Subsequently, excess HaloTag fusion protein was reacted with a biotinylated photolinker solution, successfully creating a molecule that links biotin and the HaloTag fusion protein via a photocleavable coumarin structure. SDS-PAGE was used to verify the desired conjugation by detecting coumarin-derived fluorescence in the HaloTag fusion protein band (Supplementary Figure ). To facilitate the detection of protein release efficiency, a luciferase called NanoLuc was selected as a model protein and used in the HaloTag fusion protein. Finally, the resulting conjugates were immobilized on streptavidin-binding magnetic beads to produce the photoresponsive biomaterial (7MB-9MB).