Chemical Communication between Organometallic Single-Chain Polymer Nanoparticles.

Chemical communication between macromolecules was studied by observing the controlled single chain collapse that ensues the exchange of a metal cross-linker between two polymer chains. The rhodium (I) organometallic cross-linker transfer from a low molecular weight collapsed polybutadiene to a larger polymer was followed using size exclusion chromatography. The increased effective molarity in the larger polymer seems to be the driving force for the metal migration.

Single-chain polybutadiene organometallic nanoparticles: an experimental and theoretical study.

High molecular weight polybutadienes and rhodium complexes were used to produce single chain organometallic nanoparticles. Irradiation of high -polybutadiene in the presence of a photosensitizer isomerised the double bonds to produce differing / ratios within the polymer. Notably, a higher percentage of carbon-carbon double bonds within the polymer structure led to faster binding of metal ions, as well as their faster removal by competing phosphine ligands.

Force modulated conductance of artificial coiled-coil protein monolayers.

Studies of charge transport through proteins bridged between two electrodes have been the subject of intense research in recent years. However, the complex structure of proteins makes it difficult to elucidate transport mechanisms, and the use of simple peptide oligomers may be an over simplified model of the proteins. To bridge this structural gap, we present here studies of charge transport through artificial parallel coiled-coil proteins conducted in dry environment.

De novo designed coiled-coil proteins with variable conformations as components of molecular electronic devices.

Conformational changes of proteins are widely used in nature for controlling cellular functions, including ligand binding, oligomerization, and catalysis. Despite the fact that different proteins and artificial peptides have been utilized as electron-transfer mediators in electronic devices, the unique propensity of proteins to switch between different conformations has not been used as a mechanism to control device properties and performance. Toward this aim, we have designed and prepared new dimeric coiled-coil proteins that adopt different conformations due to parallel or antiparallel relative orientations of their monomers.