Chemicals on demand with phototriggerable microcapsules.

We report the development of phototriggerable microcapsules and demonstrate the concept of protection and remote release of chemical species. Light-rupturable, liquid-filled microcapsules were prepared by coencapsulation of carbon nanotubes using a simple and robust interfacial polymerization technique. The incorporation of carbon nanotubes endows the microcapsules with the ability to respond to an external optical event.

Surface tension mediated conversion of light to work.

As energy demands increase, new, more direct, energy collection and utilization processes must be explored. We present a system that intrinsically combines the absorption of sunlight with the production of useful work in the form of locomotion of objects on liquids. Focused sunlight is locally absorbed by a nanostructured composite, creating a thermal surface tension gradient and, subsequently, motion.

Boron nitride nanotubes are noncytotoxic and can be functionalized for interaction with proteins and cells.

We report the discovery that boron nitride nanotubes (BNNTs), isosteres of CNTs with unique physical properties, are inherently noncytotoxic. Furthermore, we developed a biomemetic coating strategy to interface BNNTs with proteins and cells. Finally, we showed that BNNTs can deliver DNA oligomers to the interior of cells with no apparent toxicity.

A facile and patternable method for the surface modification of carbon nanotube forests using perfluoroarylazides.

A facile patterning method for the functionalization of vertically aligned carbon nanotubes is described. Modification of the surface of nanotube forests with hydrophilic, hydrophobic, or polymerizable small molecules was achieved via UV-triggered attachment of perfluoroarylazides. Multiple functionalizations of the tube surface can be achieved.

Design, synthesis, and biological activity of a potent Smac mimetic that sensitizes cancer cells to apoptosis by antagonizing IAPs.

Designed second mitochondrial activator of caspases (Smac) mimetics based on an accessible [7,5]-bicyclic scaffold bind to and antagonize protein interactions involving the inhibitor of apoptosis (IAP) proteins, X-chromosome-linked IAP (XIAP), melanoma IAP (ML-IAP), and c-IAPs 1 and 2 (cIAP1 and cIAP2). The design rationale is based on a combination of phage-panning data, peptide binding studies, and a survey of potential isosteres. The synthesis of two scaffolds is described.

Structure and function analysis of peptide antagonists of melanoma inhibitor of apoptosis (ML-IAP).

Melanoma inhibitor of apoptosis (ML-IAP) is a potent anti-apoptotic protein that is upregulated in a number of melanoma cell lines but not expressed in most normal adult tissues. Overexpression of IAP proteins, such as ML-IAP or the ubiquitously expressed X-chromosome-linked IAP (XIAP), in human cancers has been shown to suppress apoptosis induced by a variety of stimuli. Peptides based on the processed N-terminus of Smac/DIABLO can negate the ability of overexpressed ML-IAP or XIAP to suppress drug-induced apoptosis.