空气-水界面处β-淀粉样蛋白片层的形成。
Amyloid-beta-sheet formation at the air-water interface.
作者信息
Schladitz C, Vieira E P, Hermel H, Möhwald H
机构信息
Max-Planck-Institute for Colloids and Interfaces, Campus Golm, D-14476 Potsdam, Germany.
出版信息
Biophys J. 1999 Dec;77(6):3305-10. doi: 10.1016/S0006-3495(99)77161-4.
Abstract
An amyloid(1-40) solution rich in coil, turn, and alpha-helix, but poor in beta-sheet, develops monolayers with a high beta-sheet content when spread at the air-water interface. These monolayers are resistant to repeated compression-dilatation cycles and interaction with trifluoroethanol. The secondary structure motifs were detected by circular dichroism (CD) in solution and with infrared reflection-absorption spectroscopy (IRRAS) at the interface. Hydrophobic influences are discussed for the structure conversion in an effort to understand the completely unknown reason for the natural change of the normal prion protein cellular (PrP(C)) into the abnormal prion protein scrapie (PrP(Sc)).
摘要
富含无规卷曲、转角和α-螺旋但β-折叠较少的淀粉样蛋白（1-40）溶液，在空气-水界面铺展时会形成β-折叠含量高的单分子层。这些单分子层对反复的压缩-膨胀循环以及与三氟乙醇的相互作用具有抗性。通过溶液中的圆二色性（CD）和界面处的红外反射吸收光谱（IRRAS）检测二级结构基序。讨论了疏水作用对结构转变的影响，以努力理解正常细胞朊蛋白（PrP(C)）自然转变为异常瘙痒病朊蛋白（PrP(Sc)）这一完全未知的原因。
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