Graphene films grown on metal substrates by chemical vapor deposition (CVD) method have to be safely transferred onto desired substrates for further applications. Recently, a roll-to-roll (R2R) method has been developed for large-area transfer, which is particularly efficient for flexible target substrates. However, in the case of rigid substrates such as glass or wafers, the roll-based method is found to induce considerable mechanical damages on graphene films during the transfer process, resulting in the degradation of electrical property. Here we introduce an improved dry transfer technique based on a hot-pressing method that can minimize damage on graphene by neutralizing mechanical stress. Thus, we enhanced the transfer efficiency of the large-area graphene films on a substrate with arbitrary thickness and rigidity, evidenced by scanning electron microscope (SEM) and atomic force microscope (AFM) images, Raman spectra, and various electrical characterizations. We also performed a theoretical multiscale simulation from continuum to atomic level to compare the mechanical stresses caused by the R2R and the hot-pressing methods, which also supports our conclusion. Consequently, we believe that the proposed hot-pressing method will be immediately useful for display and solar cell applications that currently require rigid and large substrates.

Heterogeneity is essential for multicomponent lipid membranes. Especially, sterol-induced domain formation in membranes has recently attracted attention because of its biological importance. To investigate such membrane domains at the molecular level, coarse-grained molecular dynamics (CG-MD) simulations are a promising approach since they allow one to consider the temporal and spatial scales involved in domain formation. In this work, we present a new CG force field, named SPICA, which can accurately predict domain formation within various lipids in membranes. The SPICA force field was developed as an extension of a previous CG model, known as SDK (Shinoda−DeVane− Klein), in which membrane properties such as tension, elasticity, and structure are well reproduced. By examining domain formation in a series of ternary lipid bilayers, we observed a separation into liquid-ordered and liquid-disordered phases fully consistent with experimental observations. Importantly, it is shown that the SPICA force field can detect the different phase behavior that results from subtle differences in the lipid composition of the bilayer.

A coarse-grained (CG) model for peptides and proteins was developed as an extension of the Surface Property fItting Coarse grAined (SPICA) force field (FF). The model was designed to examine membrane proteins that are fully compatible with the lipid membranes of the SPICA FF. A preliminary version of this protein model was created using thermodynamic properties, including the surface tension and density in the SPICA (formerly called SDK) FF. In this study, we improved the CG protein model to facilitate molecular dynamics (MD) simulations with a reproduction of multiple properties from both experiments and all-atom (AA) simulations. An elastic network model was adopted to maintain the secondary structure within a single chain. The side-chain analogues reproduced the transfer free energy profiles across the lipid membrane and demonstrated reasonable association free energy (potential of mean force) in water compared to those from AA MD. A series of peptides/proteins adsorbed onto or penetrated into the membrane simulated by the CG MD correctly predicted the penetration depths and tilt angles of peripheral and transmembrane peptides/proteins as comparable to those in the orientations of proteins in membranes (OPM) database. In addition, the dimerization free energies of several transmembrane helices within a lipid bilayer were comparable to those from experimental estimation. Application studies on a series of membrane protein assemblies, scramblases, and poliovirus capsids demonstrated the good performance of the SPICA FF.

Amphotericin B (AmB) is a polyene macrolide antibiotic clinically used as an antifungal drug. Its preferential complexation with ergosterol (Erg), the major sterol of fungal membranes, leads to the formation of a barrel-stave-like ion channel across a lipid bilayer. To gain a better understanding of the mechanism of action, the mode of lipid bilayer spanning provides essential information. However, because of the lack of methodologies to observe it directly, it has not been revealed for the Erg-containing channel assembly for many years. In this study, we disclosed that the AmB−Erg complex spans a lipid bilayer with a single-molecule length, using solid-state nuclear magnetic resonance (NMR) experiments. Paramagnetic relaxation enhancement by Mn 2+ residing near the surface of lipid bilayers induced the depth-dependent decay of 13 C NMR signals for individual carbon atoms of AmB. We found that both terminal segments, the 41-COOH group and C38−C40 methyl groups, come close to the lipid bilayer surfaces, suggesting that the AmB−Erg complex spans a palmitoyloleoylphosphatidylcholine (POPC) bilayer with a single-molecule length. Molecular dynamics simulation experiments further confirmed the stabilization of the AmB−Erg complex as a single-length spanning complex. These results provide experimental evidence of the single-length complex incorporated in the membrane by making thinner a POPC− Erg bilayer that mimics fungal membranes.