Constructing Artificial Light-Harvesting Systems by Covalent Alignment of Aggregation-Induced Emission Molecules.

The characteristics of chloroplasts harvesting solar energy and conducting energy transfer have inspired chemists to mimic similar processes. However, accurate manipulation to gain regularly displayed antenna chromophores in mimicking chloroplasts is a great challenge. Herein, a rational design is presented that combines orderly arranged chromophores with aggregation-induced emission (AIE) to develop artificial light-harvesting systems. Tetraphenyl ethylene (TPE) molecules, which exhibited strong AIE properties, are considered as building blocks to fabricate high emissive 2D nanosheets and nanovesicles, respectively. Furthermore, the well-aligned TPE molecules are also developed as donor chromophores in light-harvesting processes. After subsequent surface modification by porphyrin molecules as acceptor chromophores, an efficient light-harvesting system has been integrally constructed. This study demonstrates a novel strategy to utilize AIE feature to mimic chloroplasts process in nature.

A highly controllable protein self-assembly system with morphological versatility induced by reengineered host-guest interactions.

Manipulating proteins to self-assemble into highly ordered nanostructures not only provides insights into the natural protein assembly process but also allows access to advanced biomaterials. Host-guest interactions have been widely used in the construction of artificial protein assemblies in recent years. CB[8] can selectively associate with two tripeptide Phe-Gly-Gly (FGG) tags with an extraordinarily high binding affinity (Kter = 1.5 × 1011 M-2). However, the FGG tags utilized before are all fixed to the N-termini via genetic fusion; this spatial limitation greatly confined the availability of the CB[8]/FGG pair in the construction of more sophisticated protein nanostructures. Here we first designed and synthesized a maleimide-functionalized Phe-Gly-Gly tag as a versatile site-specific protein modification tool; this designed tag can site-selectively introduce desired guest moieties onto protein surfaces for host-guest driven protein assembly. When regulating the self-assembly process of proteins and CB[8], the constructed protein nanosystem can exhibit distinctive morphological diversities ranging from nanorings, nanospirals, nanowires to superwires. This work developed a new strategy for site-specific protein modification of the CB[8] binding tag and provides a possible direction for the construction of 'smart', dynamic self-assembly systems.

Construction of protein assemblies by host-guest interactions with cucurbiturils.

Protein assemblies are extremely interesting in chemistry and supramolecular chemistry. How to design protein assemblies with dimensional structures is important for applications. To address this challenge, cucurbituril (CB[n]s)-based strategies have been explored owing to their high affinity toward small peptide motifs, organic cations and amines. By incorporation of a small molecule guest and a peptide motif guest into N-terminals of oligomeric proteins, CB[n]s could recognize and bind to the N-terminal guests, leading to dimensional protein assemblies. The dimensional protein assemblies possess structural, stimuli-responsive and bioactive properties with great potential for in vivo applications. Herein, we reviewed the progress in the design of dimensional protein assemblies based on supramolecular interactions of CB[n]s and present the perspectives in the design of high-ordered biomaterials for biomedical applications.

Selenium-containing organic nanoparticles as silent precursors for ultra-sensitive thiol-responsive transmembrane anion transport.

An anion transporter with a selenoxide group was able to form nanoparticles in water, whose activity was fully turned off due to the aggregation effect. The formed nanoparticles have a uniform size and can be readily dispersed in water at high concentrations. Turn-on of the nanoparticles by reducing molecules is proposed to be a combined process, including the reduction of selenoxide to selenide, disassembly of the nanoparticles and location of the transporter to the lipid membrane. Accordingly, a special acceleration phase can be observed in the turn-on kinetic curves. Since turn-on of the nanoparticles is quantitatively related to the amount of reductant, the nanoparticles can be activated in a step-by-step manner. Due to the sensibility of this system to thiols, cysteine can be detected at low nanomolar concentrations. This ultra-sensitive thiol-responsive transmembrane anion transport system is quite promising in biological applications.

Construction of supramolecular polymer by enzyme-triggered covalent condensation of CB[8]-FGG-based supramonomer.

A rapid and effective enzymatic strategy for the fabrication of a supramolecular polymer is presented for the first time, in which a bifunctional ternary host-guest supramonomer is first prepared followed by subsequent enzymatic coupling of supramonomers.

Redox control of GPx catalytic activity through mediating self-assembly of Fmoc-phenylalanine selenide into switchable supramolecular architectures.

Artificial enzymes capable of achieving tunable catalytic activity through stimuli control of enzymatic structure transition are of significance in biosensor and biomedicine research. Herein we report a novel smart glutathione peroxidise (GPx) mimic with modulatory catalytic activity based on redox-induced supramolecular self-assembly. First, an amphiphilic Fmoc-phenylalanine-based selenide was designed and synthesized, which can self-assemble into nanospheres (NSs) in aqueous solution. The NSs demonstrate extremely low GPx activity. Upon the oxidation of hydroperoxides (ROOH), the selenide can be quickly transformed into the selenoxide form. The change of the molecular structure induces complete morphology transition of the self-assemblies from NSs to nanotubes (NTs), resulting in great enhancement in the GPx catalytic activity. Under the reduction of GSH, the selenoxide can be further reversibly reduced back into the selenide; therefore the reversible switch between the NSs and NTs can be successfully accomplished. The relationship between the catalytic activity and enzymatic structure was also investigated. The dual response nature makes this mimic play roles of both a sensor and a GPx enzyme at the same time, which can auto-detect the signal of ROOH and then auto-change its activity to achieve quick or slow/no scavenging of ROOH. The dynamic balance of ROOH is vital in organisms, in which an appropriate amount of ROOH does benefit to the metabolism, whereas surplus ROOH can cause oxidative damage of the cell instead and this smart mimic is of remarkable significance. We expect that such a mimic can be developed into an effective antioxidant drug and provide a new platform for the construction of intelligent artificial enzymes with multiple desirable properties.

Self-assembly of amphiphilic peptides into bio-functionalized nanotubes: a novel hydrolase model.

Herein, we report the construction of a novel hydrolase model via self-assembly of a synthetic amphiphilic short peptide (Fmoc-FFH-CONH2) into nanotubes. The peptide-based self-assembled nanotubes (PepNTs-His) with imidazolyl groups as the catalytic centers exhibit high catalytic activity for p-nitrophenyl acetate (PNPA) hydrolysis. By replacement of the histidine of Fmoc-FFH-CONH2 with arginine to produce a structurally similar peptide Fmoc-FFR-CONH2, guanidyl groups can be presented in the nanotubes through the co-assembly of these two molecules to stabilize the transition state of the hydrolytic reaction. Therefore significantly improved catalytic activity has been achieved by the reasonable distribution of three dominating catalytic factors: catalytic center, binding site and transition state stabilization to the co-assembled peptide nanotubes (PepNTs-His-Argmax). The resulting hydrolase model shows typical saturation kinetics behaviour to that of natural enzymes and the catalytic efficiency of a single catalytic center is 519-fold higher than that without catalysts. As for a nanotube with multi-catalytic centers, a remarkable catalytic efficiency could be achieved with the increase of building blocks. This model suggests that the well ordered and dynamic supramolecular structure is an attractive platform to develop new artificial enzymes to enhance the catalytic activity. Besides, this novel peptide-based material has excellent biocompatibility with human cells and is expected to be applied to organisms as a substitute for natural hydrolases.