Epitaxial growth of topological insulator Bi2Se3 film on Si(111) with atomically sharp interface

Atomically sharp epitaxial growth of Bi2Se3 films is achieved on Si (111) substrate with MBE (Molecular Beam Epitaxy). Two-step growth process is found to be a key to achieve interfacial-layer-free epitaxial Bi2Se3 films on Si substrates. With a single-step high temperature growth, second phase clusters are formed at an early stage. On the other hand, with low temperature growth, the film tends to be disordered even in the absence of a second phase. With a low temperature initial growth followed by a high temperature growth, second-phase-free atomically sharp interface is obtained between Bi2Se3 and Si substrate, as verified by RHEED (Reflection High Energy Electron Diffraction), TEM (Transmission Electron Microscopy) and XRD (X-Ray Diffraction). The lattice constant of Bi2Se3 is observed to relax to its bulk value during the first quintuple layer according to RHEED analysis, implying the absence of strain from the substrate. TEM shows a fully epitaxial structure of Bi2Se3 film down to the first quintuple layer without any second phase or an amorphous layer.Comment: 20 pages, 7 figure

Understanding the Structure–Function Relationship of Lysozyme Resistance in Staphylococcus aureus by Peptidoglycan O‑Acetylation Using Molecular Docking, Dynamics, and Lysis Assay

Lysozyme is an important component of the host innate defense system. It cleaves the β-1,4 glycosidic bonds between <i>N</i>-acetylmuramic acid and <i>N</i>-acetylglucosamine of bacterial peptidoglycan and induce bacterial lysis. Staphylococcus aureus (S. aureus), an opportunistic commensal pathogen, is highly resistant to lysozyme, because of the O-acetylation of peptidoglycan by <i>O</i>-acetyl transferase (<i>oatA</i>). To understand the structure–function relationship of lysozyme resistance in S. aureus by peptidoglycan O-acetylation, we adapted an integrated approach to (i) understand the effect of lysozyme on the growth of S. aureus parental and the <i>oatA</i> mutant strain, (ii) study the lysozyme induced lysis of exponentially grown and stationary phase of both the S. aureus parental and <i>oatA</i> mutant strain, (iii) investigate the dynamic interaction mechanism between normal (de-O-acetylated) and O-acetylated peptidoglycan substrate in complex with lysozyme using molecular docking and molecular dynamics simulations, and (iv) quantify lysozyme resistance of S. aureus parental and the <i>oatA</i> mutant in different human biological fluids. The results indicated for the first time that the active site cleft of lysozyme binding with O-acetylated peptidoglycan in S. aureus was sterically hindered and the structural stability was higher for the lysozyme in complex with normal peptidoglycan. This could have conferred reduced survival of the S. aureus <i>oatA</i> mutant in different human biological fluids. Consistent with this computational analysis, the experimental data confirmed decrease in the growth, lysozyme induced lysis, and lysozyme resistance, due to peptidoglycan O<i>-</i>acetylation in S. aureus