The purpose of the present study is to develop computational systems available for the design of mechanical sensors using conducting polymers. Numerical studies have been conducted, using simplified beam modeling and electrochemical-mechanical modeling. The beam modeling is simple, but inaccurate for multi-step response. The electrochemical-mechanical modeling is complicated, but accurate even for multi-step response.[This abstract is not included in the PDF]
Recently, an amorphous structure named “photonic amorphous diamond (PAD)” has been found by numerical calculations to form a sizable three-dimensional photonic band-gap (3D-PBG), despite the complete absence of lattice periodicity. In this article, we review our recent experimental study on the 3D-PBG formation and light propagation properties in PAD.
There have been many reports suggesting that soluble oligomers of amyloid β (Aβ) are neurotoxins causing Alzheimer's disease (AD). Although inhibition of the soluble oligomerization of Aβ is considered to be effective in the treatment of AD, almost all peptide inhibitors have been designed from the β-sheet structure (H14-D23) of Aβ1-42. To obtain more potent peptides than the known inhibitors of the soluble-oligomer formation of Aβ1-42, we performed random screening by phage display. After fifth-round panning of a hepta-peptide library against soluble Aβ1-42, novel peptides containing arginine residues were enriched. These peptides were found to suppress specifically 37/48 kDa oligomer formation and to keep the monomeric form of Aβ1-42 even after 24 h of incubation, as disclosed by SDS-PAGE and size-exclusion chromatography. Thus we succeeded in acquiring novel efficient peptides for inhibition of soluble 37/48 kDa oligomer formation of Aβ1-42.