title: Protein-responsive assemblies from catechol-metal ion supramolecular coordination.
abstract: Supramolecular self-assembly driven by catechol-metal ion coordination has gained great success in the fabrication of functional materials including adhesives, capsules, coatings and hydrogels. However, this route has encountered a great challenge in the construction of nanoarchitectures in the absence of removable templates, because of the uncontrollable crosslinking of catechol-metal ion coordination. Herein, we show that a supramolecular approach, combining both catechol-metal ion coordination and polymer self-assembly together, can organize polymers into hybrid nanoassemblies ranging from solid particles, homogeneous vesicles to Janus vesicles. Without the introduction of a specific binding ligand or complicated molecular design, these assemblies can totally disassemble in response to proteins. UV/vis absorption, fluorescence quenching and recovery investigations have confirmed that proteins can seize metal ions from the hybrid nanoassemblies, thus causing the degradation of catechol-metal ion coordination networks.
authors: College of Materials, Xiamen University, Xiamen, 361005, China.
authors: C
authors: C
authors: Yuan
authors: J
authors: J
authors: Chen
authors: S
authors: S
authors: Yu
authors: Y
authors: Y
authors: Chang
authors: J
authors: J
authors: Mao
authors: Y
authors: Y
authors: Xu
authors: W
authors: W
authors: Luo
authors: B
authors: B
authors: Zeng
authors: L
authors: L
authors: Dai
mesh_terms: D000818:Animals; D002396:Catechols / Q000737:chemistry*; D002417:Cattle; D007477:Ions; D007501:Iron / Q000737:chemistry; D008670:Metals / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry / Q000648:ultrastructure; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D014357:Trypsin / Q000737:chemistry*
chemical_list: D002396:Catechols; D007477:Ions; D008670:Metals; D012710:Serum Albumin, Bovine; D007501:Iron; D014357:Trypsin; C034221:catechol