Chemical engineering of self-assembled Alzheimer's peptide on a silanized silicon surface

The aim of this work is to develop a sensitive and specific immune-sensing platform dedicated to the detection of potential biomarkers of Alzheimer's disease (AD) in biological fluids. Accordingly, a controlled and adaptive surface functionalization of a silicon wafer with 7-octenyltrichlorosil...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 30(2014), 20 vom: 27. Mai, Seite 5863-72
1. Verfasser: Ammar, Mehdi (VerfasserIn)
Weitere Verfasser: Smadja, Claire, Ly, Giang Thi Phuong, Tandjigora, Diénaba, Vigneron, Jackie, Etcheberry, Arnaud, Taverna, Myriam, Dufour-Gergam, Elisabeth
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't 7-octenyltrichlorosilane Amyloid beta-Peptides Immunoglobulin G Peptide Fragments Silanes amyloid beta-protein (1-42) Silicon Z4152N8IUI
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245 1 0 |a Chemical engineering of self-assembled Alzheimer's peptide on a silanized silicon surface 
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520 |a The aim of this work is to develop a sensitive and specific immune-sensing platform dedicated to the detection of potential biomarkers of Alzheimer's disease (AD) in biological fluids. Accordingly, a controlled and adaptive surface functionalization of a silicon wafer with 7-octenyltrichlorosilane has been performed. The surface has extensively been characterized by atomic force microscopy (AFM; morphology) and X-ray photoelectron spectroscopy (XPS; chemical composition) and contact angle measurements. The wettability of the grafted chemical groups demonstrated the gradual trend from hydrophilic to hydrophobic surface during functionalization. XPS evidenced the presence of silanes on the surface after silanization, and even carboxylic groups as products from the oxidation step of the functionalization process. The characterization results permitted us to define an optimal protocol to reach a high-quality grafting yield. The issue of the quality of controlled chemical preparation on bioreceiving surfaces was also investigated by the recognition of one AD biomarker, the amyloid peptide Aβ 1-42. We have therefore evaluated the biological activity of the grafted anti Aβ antibodies onto this silanized surface by fluorescent microscopy. In conclusion, we have shown, both qualitatively and quantitatively, the uniformity of the optimized functionalization on slightly oxidized silicon surfaces, providing a reliable and chemically stable procedure to determine specific biomarkers of Alzheimer disease. This work opens the route to the integration of controlled immune-sensing applications on lab-on-chip systems 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a 7-octenyltrichlorosilane  |2 NLM 
650 7 |a Amyloid beta-Peptides  |2 NLM 
650 7 |a Immunoglobulin G  |2 NLM 
650 7 |a Peptide Fragments  |2 NLM 
650 7 |a Silanes  |2 NLM 
650 7 |a amyloid beta-protein (1-42)  |2 NLM 
650 7 |a Silicon  |2 NLM 
650 7 |a Z4152N8IUI  |2 NLM 
700 1 |a Smadja, Claire  |e verfasserin  |4 aut 
700 1 |a Ly, Giang Thi Phuong  |e verfasserin  |4 aut 
700 1 |a Tandjigora, Diénaba  |e verfasserin  |4 aut 
700 1 |a Vigneron, Jackie  |e verfasserin  |4 aut 
700 1 |a Etcheberry, Arnaud  |e verfasserin  |4 aut 
700 1 |a Taverna, Myriam  |e verfasserin  |4 aut 
700 1 |a Dufour-Gergam, Elisabeth  |e verfasserin  |4 aut 
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