An Intramolecular O−N Migration Reaction on Gold Surfaces: Toward the Preparation of Well-Defined Amyloid Surfaces Export

@article{Boussert2009, abstract = {PMID: 19772298 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).}, author = {Boussert, Stephanie and Diez-Perez, Ismael and Kogan, Marcelo J. and de Oliveira, Eliandre and Giralt, Ernest}, citeulike-article-id = {6017935}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/nn900935p}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/nn900935p}, day = {27}, doi = {10.1021/nn900935p}, journal = {ACS Nano}, keywords = {amyloid, beta-hairpin, chemistry, fibrils, peptide-design, surfaces}, month = {October}, number = {10}, pages = {3091--3097}, posted-at = {2009-10-28 10:27:49}, priority = {4}, title = {An Intramolecular O−N Migration Reaction on Gold Surfaces: Toward the Preparation of Well-Defined Amyloid Surfaces}, url = {http://dx.doi.org/10.1021/nn900935p}, volume = {3}, year = {2009} }

TY - JOUR ID - Boussert2009 L3 - citeulike-article-id:6017935 N2 - PMID: 19772298 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). IS - 10 JF - ACS Nano EP - 3097 TI - An Intramolecular O−N Migration Reaction on Gold Surfaces: Toward the Preparation of Well-Defined Amyloid Surfaces VL - 3 SP - 3091 KW - amyloid KW - beta-hairpin KW - chemistry KW - fibrils KW - peptide-design KW - surfaces AU - Boussert, Stephanie AU - Diez-Perez, Ismael AU - Kogan, Marcelo AU - de Oliveira, Eliandre AU - Giralt, Ernest PY - 2009/10/27/ UR - http://dx.doi.org/10.1021/nn900935p ER -