4.6 Article

Comprehensive Characterization of APTES Surface Modifications of Hydrous Boehmite Nanoparticles

Journal

LANGMUIR
Volume 37, Issue 1, Pages 171-179

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.langmuir.0c02682

Keywords

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Funding

  1. Deutsche Forschungsgemeinschaft (DFG) [GA 1492/10-2, STU 245/5-2]

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The study demonstrates that adjusting the surface properties of nanofillers allows for selectively designing interactions to optimize the advantages of nanocomposites. By using specific process parameters, a monolayer can be formed on BNP, resulting in a maximal grafting density of 1.3 molecules/nm^2. Unsuspected multilayer formation is observed only under acidic conditions.
Hydrous boehmite (gamma-AlOOH) nanoparticles (BNP) show great potential as nanoscale filler for the fabrication of fiber reinforced nanocomposite materials. Notably, the particle- matrix interaction has been demonstrated to be decisive for improving the matrix-dominant mechanical properties in the past years. Tailoring the surface properties of the nanofiller enables to selectively design the interaction and thus to exploit the benefits of the nanocomposite in an optimal way. Here, an extensive study is presented on the binding of (3-aminopropyl)triethoxysilane (APTES), a common silane surface modifier, on BNP in correlation to different process parameters (concentration, time, temperature, and pH). Furthermore, a comprehensive characterization of the modified BNP was performed by using elemental analysis (EA), thermogravimetric analysis (TGA) coupled with mass spectrometry (TGA-MS), and Kaiser's test (KT). The results show an increasing monolayer formation up to a complete surface coverage with rising APTES concentration, time, and temperature, resulting in a maximal grafting density of 1.3 molecules/nm(2). Unspecific multilayer formation was solely observed under acidic conditions. Comparison of TGA-MS results with data recorded from EA, TGA, and KT verified that TGA-MS is a convenient and highly suitable method to elucidate the ligand binding in detail.

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