ABSTRACT
In this contribution a convenient synthetic method to obtain tetraacylgermanes Ge[C(O)R]4 (R=mesityl (1 a), phenyl (1 b)), a previously unknown class of highly efficient Ge-based photoinitiators, is described. Tetraacylgermanes are easily accessible via a one-pot synthetic protocol in >85 % yield, as confirmed by NMR spectroscopy, mass spectrometry, and X-ray crystallography. The efficiency of 1 a,b as photoinitiators is demonstrated in photobleaching (UV/Vis), time-resolved EPR (CIDEP), and NMR/CIDNP investigations as well as by photo-DSC studies. Remarkably, the tetraacylgermanes exceed the performance of currently known long-wavelength visible-light photoinitiators for free-radical polymerization.
ABSTRACT
The synthesis of redox-active p- and o-quinones 2-phenylamino-4-phenylimino[6]helicene-1-one 1, 2-phenylamino[6]-helicene-1,4-dione 2, and 4-phenyl[6]helicene-1,2-dione 3 in their enantiopure forms by post-functionalization of (P)- and (M)-1,2-dimethoxy[6]helicene is presented. Structural characterization in solution and in the solid state was accomplished by 2D NMR spectroscopy methods and X-ray diffraction analysis, respectively. Interpretation of electrochemical redox data was accompanied by a detailed orbital picture, derived from DFT calculations. The electronic structures of compounds 1-3 were investigated by UV/Vis and electronic circular dichroism (ECD) spectroscopy, complemented by TD-DFT calculations. Quinones 1-3 were chemically reduced to study the EPR signatures of their respective radical anions. DFT methods were used for the atom assignment of the hyperfine coupling constants. The results are discussed within the context of electrochromic chiral switches and molecular recognition.
ABSTRACT
In this study, we demonstrate that emulsified microemulsions and micellar cubosomes are suitable as sustained delivery vehicles for water-soluble proteins. Through structural modifications, the loading efficiency of two model proteins, namely bovine serum albumin (BSA) and cytochrome c could be remarkably increased. A procedure for preparing these particles loaded with optimized amounts of sensitive substances is presented. Loading and dispersion at low temperatures is performed in two successive steps. First, a water-in-oil microemulsion is loaded with the proteins. Subsequently, this phase is dispersed in water resulting in particles with microemulsion and micellar cubic internal structure and a size of approximately 620 nm. This two-step method ensures optimal loading of the particles with the proteins. These nanostructured particles are able to sustain the release of the water-soluble BSA and cytochrome c. Within one day, less than 10% of BSA and 15% of cytochrome c are released. The release rate of cytochrome c is influenced by the nanostructure of the particles.
