Graphene sheets as anode materials for Li-ion batteries: Preparation, structure, electrochemical properties and mechanism for lithium storage

10.1039/c2ra20549aRSC Advances2176792-679

Novel Two-Stage Analytic Approach in Extraction of Strong Herb-Herb Interactions in TCM Clinical Treatment of Insomnia

2nd International Conference on Medical Biometrics, ICMB 2010, Hong Kong, China, Jun 28-30, 2010In this paper, we aim to investigate strong herb-herb interactions in TCM for effective treatment of insomnia. Given that extraction of herb interactions is quite similar to gene epistasis study due to non-linear interactions among their study factors, we propose to apply Multifactor Dimensionality Reduction (MDR) that has shown useful in discovering hidden interaction patterns in biomedical domains. However, MDR suffers from high computational overhead incurred in its exhaustive enumeration of factors combinations in its processing. To address this drawback, we introduce a two-stage analytical approach which first uses hierarchical core sub-network analysis to pre-select the subset of herbs that have high probability in participating in herb-herb interactions, which is followed by applying MDR to detect strong attribute interactions in the pre-selected subset. Experimental evaluation confirms that this approach is able to detect effective high order herb-herb interaction models in high dimensional TCM insomnia dataset that also has high predictive accuracies.Department of Health Technology and InformaticsRefereed conference pape

Atomic-Scale Simulations Confirm that Soluble β-Sheet-Rich Peptide Self-Assemblies Provide Amyloid Mimics Presenting Similar Conformational Properties

The peptide self-assembly mimic (PSAM) from the outer surface protein A (OspA) can form highly stable but soluble β-rich self-assembly-like structures similar to those formed by native amyloid-forming peptides. However, unlike amyloids that predominantly form insoluble aggregates, PSAMs are highly water-soluble. Here, we characterize the conformations of these soluble β-sheet-rich assemblies. We simulate PSAMs with different-sized β-sheets in the presence and absence of end-capping proteins using all-atom explicit-solvent molecular dynamics, comparing the structural stability, conformational dynamics, and association force. Structural and free-energy comparisons among β-sheets with different numbers of layers and sequences indicate that in similarity to amyloids, the intersheet side chain-side chain interactions and hydrogen bonds combined with intrasheet salt bridges are the major driving forces in stabilizing the overall structural organization. A detailed structural analysis shows that in similarity to amyloid fibrils, all wild-type and mutated PSAM structures display twisted and bent β-sheets to some extent, implying that a twisted and bent β-sheet is a general motif of β-rich assemblies. Thus, our studies indicate that soluble β-sheet-rich peptide self-assemblies can provide good amyloid mimics, and as such confirm on the atomic scale that they are excellent systems for amyloid studies. These results provide further insight into the usefulness of such mimics for nanostructure design