本研究では，導電性高分子を利用した力学センサの設計に有用な汎用的計算システムの開発を目的とし，簡易はりモデルおよび電気化学・力学モデルによる試計算を実施した．前者は簡単だが，多段応答の精度が悪い．後者は複雑だが，多段応答の精度が改善される．［本要旨はPDFには含まれない］

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最近, 格子周期性を全く持たないにもかかわらず, 大きな3次元の光禁制帯 (3D-PBG) を形成する フォトニック・アモルファス・ダイアモンド (PAD) とよばれる構造が, 数値計算により発見された. 本稿では, PADにおける3D-PBG形成と光伝播特性について実験的に調べた最近の我々の研究について解説する.

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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 Aβ_1-42. To obtain more potent peptides than the known inhibitors of the soluble-oligomer formation of Aβ_1-42, we performed random screening by phage display. After fifth-round panning of a hepta-peptide library against soluble Aβ_1-42, 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 Aβ_1-42 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 Aβ_1-42.

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