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We investigate the photocatalytic performance of nanocomposites prepared in a one-step process by liquid-phase exfoliation of graphite in the presence of TiO$_2$ nanoparticles (NPs) at atmospheric pressure and in water, without heating or adding any surfactant, and starting from low-cost commercial reagents. The nanocomposites show enhanced photocatalytic activity, degrading up to 40$\%$ more pollutants with respect to the starting TiO$_2$-NPs. In order to understand the photo-physical mechanisms underlying this enhancement, we investigate the photo-generation of reactive species (trapped holes and electrons) by ultrafast transient absorption spectroscopy. We observe an electron transfer process from TiO$_2$ to the graphite flakes within the first picoseconds of the relaxation dynamics, which causes the decrease of the charge recombination rate, and increases the efficiency of the reactive species photo-production., Comment: 13 pages, 12 figures, 1 table

In this study, native chemical ligation (NCL) was used as a selective cross-linking method to form core-cross-linked thermosensitive polymeric micelles for drug delivery applications. To this end, two complementary ABA triblock copolymers having polyethylene glycol (PEG) as midblock were synthesized by atom transfer radical polymerization (ATRP). The thermosensitive poly isopropylacrylamide (PNIPAM) outer blocks of the polymers were copolymerized with either N-(2-hydroxypropyl)methacrylamide-cysteine (HPMA-Cys), P(NIPAM-co-HPMA-Cys)-PEG-P(NIPAM-co-HPMA-Cys) (PNC) or N-(2-hydroxypropyl)methacrylamide-ethylthioglycolate succinic acid (HPMA-ETSA), P(NIPAM-co-HPMA-ETSA)-PEG-P(NIPAM-co-HPMA-ETSA) (PNE). Mixing of these polymers in aqueous solution followed by heating to 50 °C resulted in the formation of thermosensitive flower-like micelles. Subsequently, native chemical ligation in the core of micelles resulted in stabilization of the micelles with a Z-average of 65 nm at body temperature. Decreasing the temperature to 10 °C only affected the size of the micelles (increased to 90 nm) but hardly affected the polydispersity index (PDI) and aggregation number (Nagg) confirming covalent stabilization of the micelles by NCL. CryoTEM images showed micelles with an uniform spherical shape and dark patches close to the corona of micelles were observed in the tomographic view. The dark patches represent more dense areas in the micelles which coincide with the higher content of HPMA-Cys/ETSA close to the PEG chain revealed by the polymerization kinetics study. Notably, this cross-linking method provides the possibility for conjugation of functional molecules either by using the thiol moieties still present after NCL or by simply adjusting the molar ratio between the polymers (resulting in excess cysteine or thioester moieties) during micelle formation. Furthermore, in vitro cell experiments demonstrated that fluorescently labeled micelles were successfully taken up by HeLa cells while cell viability remained high even at high micelle concentrations. These results demonstrate the potential of these micelles for drug delivery applications.

Viruses are among the simplest biological systems and are highly effective vehicles for the delivery of genetic material into susceptible host cells1. Artificial viruses can be used as model systems for providing insights into natural viruses and can be considered a testing ground for developing artificial life. Moreover, they are used in biomedical and biotechnological applications, such as targeted delivery of nucleic acids for gene therapy1, 2 and as scaffolds in material science3, 4, 5. In a natural setting, survival of viruses requires that a significant fraction of the replicated genomes be completely protected by coat proteins. Complete protection of the genome is ensured by a highly cooperative supramolecular process between the coat proteins and the nucleic acids, which is based on reversible, weak and allosteric interactions only6, 7, 8, 9. However, incorporating this type of supramolecular cooperativity into artificial viruses remains challenging10, 11, 12, 13, 14, 15. Here, we report a rational design for a self-assembling minimal viral coat protein based on simple polypeptide domains. Our coat protein features precise control over the cooperativity of its self-assembly with single DNA molecules to finally form rod-shaped virus-like particles. We confirm the validity of our design principles by showing that the kinetics of self-assembly of our virus-like particles follows a previous model developed for tobacco mosaic virus9. We show that our virus-like particles protect DNA against enzymatic degradation and transfect cells with considerable efficiency, making them promising delivery vehicles.

Viruses are among the simplest biological systems and are highly effective vehicles for the delivery of genetic material into susceptible host cells. Artificial viruses can be used as model systems for providing insights into natural viruses and can be considered a testing ground for developing artificial life. Moreover, they are used in biomedical and biotechnological applications, such as targeted delivery of nucleic acids for gene therapy and as scaffolds in material science. In a natural setting, survival of viruses requires that a significant fraction of the replicated genomes be completely protected by coat proteins. Complete protection of the genome is ensured by a highly cooperative supramolecular process between the coat proteins and the nucleic acids, which is based on reversible, weak and allosteric interactions only. However, incorporating this type of supramolecular cooperativity into artificial viruses remains challenging. Here, we report a rational design for a self-assembling minimal viral coat protein based on simple polypeptide domains. Our coat protein features precise control over the cooperativity of its self-assembly with single DNA molecules to finally form rod-shaped virus-like particles. We confirm the validity of our design principles by showing that the kinetics of self-assembly of our virus-like particles follows a previous model developed for tobacco mosaic virus. We show that our virus-like particles protect DNA against enzymatic degradation and transfect cells with considerable efficiency, making them promising delivery vehicles.

Dual labeled liposomes, carrying both paramagnetic and fluorescent lipids, were recently proposed as potent contrast agents for MR molecular imaging. These nanoparticles are coated with poly(ethylene glycol) (PEG) to increase their blood circulation half-life, which should allow extensive accumulation at the targeted site. To eliminate nonspecific blood pool signal from the MR images, the circulating liposomes should ideally be cleared from the circulation when sufficient target-specific contrast enhancement is obtained. To that aim, we designed an avidin chase that allowed controlled and rapid clearance of paramagnetic biotinylated liposomes from the blood circulation in C57BL/6 mice. Avidin-induced alterations in blood clearance kinetics and tissue distribution were studied quantitatively by determination of the Gd content in blood and tissue samples ex vivo. Intrinsic liposomal blood clearance showed bi-exponential behavior with half-lives t(1/2alpha) = 2.1 +/- 1.1 and t(1/2beta) = 15.1 +/- 5.4 hours, respectively. In contrast, the contrast agent was cleared from the blood by the avidin infusion to

This is the result of an ongoing collaboration with Dr. N. Sommerdijk’s Biomaterials group at the University of Eindhoven (the Netherlands) and illustrates the close collaboration that exists in pursuing the design and application of novel polymeric materials between the two groups. This details work on a physical phenomenon (selective delamination) and key materials (amphiphilic block copolymers) that have subsequently been applied in the design of novel biomaterials. These results have appeared in a larger body of work including Advanced Materials, Angewandtie Chemie International Edition and the Journal of Materials Chemistry.

Type I collagen is a major constituent of many biological tissues, including skin, bone, tendon and cartilages. Its main functions are to shape extracellular matrices, promote cell attachment and provide tissues with strength, flexibility and elasticity. At the core these functions is its remarkable ability of collagen to form highly organized fibrils through the self-assembly of the molecules. The fibrilogenesis involves the lateral association of collagen triple helices into staggered parallel arrays that give rise to the characteristic D-band periodicity of 67 nm. Currently, the mechanisms of collagen self-assembly are poorly understood. Here, we combine the nanometer-scale resolution of cryo-transmission electron microscopy (cryoTEM) with molecular dynamics to investigate the self-assembly of collagen molecules into fibrils in solution.