Fiona Wang

© 2016 American Chemical Society.High quality WSe2 films have been grown on bilayer graphene with layer-by-layer control of thickness using molecular beam epitaxy. The combination of angle-resolved photoemission, scanning tunneling microscopy/spectroscopy, and optical absorption measurements reveal the atomic and electronic structures evolution and optical response of WSe2/BLG. We observe that a bilayer of WSe2 is a direct bandgap semiconductor, when integrated in a BLG-based heterostructure, thus shifting the direct-indirect band gap crossover to trilayer WSe2. In the monolayer limit, WSe2 shows a spin-splitting of 475 meV in the valence band at the K point, the largest value observed among all the MX2 materials. The exciton binding energy of monolayer-WSe2/BLG is found to be 0.21 eV, a value that is orders of magnitude larger than that of conventional three-dimensional semiconductors, yet small as compared to other two-dimensional transition metal dichalcogennides semiconductors. Finally, our finding regarding the overall modification of the electronic structure by an alkali metal surface electron doping opens a route to further control the electronic properties of TMDCs.

Cholesteryl ester transfer protein mediates the transfer of cholesterol esters from atheroprotective high-density lipoproteins to atherogenic low-density lipoproteins. CETP inhibition has been regarded as a promising strategy for increasing HDL levels and subsequently reducing the risk of cardiovascular diseases. Although the crystal structure of CETP is known, little is known regarding how CETP binds to HDL. Here, we investigated how various HDL-like particles interact with CETP by electron microscopy and molecular dynamics simulations. Results showed that CETP binds to HDL via hydrophobic interactions rather than protein-protein interactions. The HDL surface lipid curvature generates a hydrophobic environment, leading to CETP hydrophobic distal end interaction. This interaction is independent of other HDL components, such as apolipoproteins, cholesteryl esters and triglycerides. Thus, disrupting these hydrophobic interactions could be a new therapeutic strategy for attenuating the interaction of CETP with HDL.