An Intramolecular O−N Migration Reaction on Gold Surfaces: Toward the Preparation of Well-Defined Amyloid Surfaces
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- 作者：Stephanie Boussert ; Ismael Diez-Perez ; Marcelo J. Kogan ; Eliandre de Oliveira ; Ernest Giralt
- 刊名：ACS Nano
- 出版年：2009
- 出版时间：October 27, 2009
- 年：2009
- 卷：3
- 期：10
- 页码：3091-3097
- 全文大小：375K
- 年卷期：0
- ISSN：1936-086X
文摘
Amyloids are a family of self-aggregating proteins implicated in various central nervous system disorders, including Alzheimer’s disease (AD). It is thought that prefibrillar soluble forms of amyloid peptides, including oligomers, may be the main pathogenic factor in AD. Herein we describe the fabrication of well-defined, functionalized, monomeric β-amyloid peptide surfaces for studying protein−protein interactions. We first prepared a nonaggregating analogue of the β-amyloid peptide and then attached it to a gold surface covered with a self-assembled monolayer (SAM) of alkanethiols. After attachment, the native form of the β-amyloid peptide (Aβ40) was obtained by surface-level intramolecular O−N migration. The surface was characterized by atomic force microscopy (AFM) and self-assembled monolayer for matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (SAMDI-TOF MS). The interaction between the surface-bound Aβ40 and monoclonal anti-Aβ40 antibody was tracked by AFM and chemiluminescence, which revealed that the Aβ40 was attached mainly in its monomeric form and that the protein−protein complex was assembled on the surface. Last, we used a proteomics approach to demonstrate the specificity of the Aβ40-functionalized surface in surface-binding experiments employing serum amyloid P (SAP) and bovine serum albumin (BSA).