著者
渡邉 亜沙子 岡畑 恵雄 古澤 宏幸 星 美奈子 櫻井 実
出版者
低温生物工学会
雑誌
低温生物工学会誌 (ISSN:13407902)
巻号頁・発行日
vol.51, no.2, pp.137-140, 2005-12-30 (Released:2017-06-19)
参考文献数
3
被引用文献数
1

The effect of trehalose on the aggregation of β-amyloid (Aβ) was investigated using quartz crystal microbalance (QCM) and circular dichroism spectroscopy (CD). Here we prepared three types of host Aβ-guest Aβ systems differing in a combination of their secondary structures: namely, β-sheet-β-sheet (system (1)), β-sheet-random coil (system(2)) and random coil-random coil (system(3)). The host Aβ was fixed on the electrode of QCM, and the guest Aβ was dissolved in a buffer solution. The host-guest interaction was monitored through a frequency shift (ΔF) of the quartz vibration: a larger ΔF value means the occurrence of a larger degree of host-guest aggregation. When disaccharide (trehalose, neotrehalose or maltose) was added in the above system, the time dependent profile of ΔF was significantly affected. In systems (1) and (2), any of these disaccharides depressed significantly the host-guest aggregation: maltose and trehalose exhibited the strongest effect in systems (1) and (2), respectively. Interestingly, in system(3), trehalose rather promoted the aggregation compared with the control (without disaccharide), while both maltose and neotrehalose depressed the aggregation as much as in the cases of systems (1) and (2). The results of systems (2) and (3) imply that trehalose more strongly interacts with Aβ in a random coil than that in p-sheets. In fact, CD measurements indicated that trehalose retarded the transformation of Aβ from a random coil to β-sheet. Taken together, these results open up the possibility that trehalose modifies the aggregation process of Aβ through its preferential interaction with the random coil state of Aβ.
著者
大川 拓 黄川田 隆洋 奥田 隆 櫻井 実
出版者
低温生物工学会
雑誌
低温生物工学会誌 (ISSN:13407902)
巻号頁・発行日
vol.56, no.1, pp.39-42, 2010-03-15

Here the three-dimensional (3-D) structure of TRET1, a novel trehalose transporter from an anhydrobiotic insect, Polypedilum vanderplanki, was predicted by homology modeling in which the 3-D structure (1SUK) of GLUT1, glucose transporter from human was selected as a template. It was found that TRET1 has 12 transmembrane (TM) helices with an inward-facing conformation. Next, to explore the dynamics of the protein, we performed molecular dynamics (MD) simulation for the protein embedded in a hydrated phospholipid bilayer. The result of principal component analysis indicated that the protein has a hinge-bending motion, that is, the helices on the intracellular side come close or draw apart together. This dynamics may be essential for substrate uptake. Furthermore, we performed docking simulation combined with binding energy calculation to investigate the substrate selectivity of TRET1. As a result, it was found that trehalose more strongly binds to TRET1 than its isomer, isotrehalose, consistent with available experimental data.