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Microcontact printing of Alzheimer’s β-amyloid monomers and fibrils

Year: 2013

Journal: European Polymer Journal, Volume 49, Issue 10, October 2013, Pages 3052–3059, 20131119

Authors: Danting Huang 1 2,, Zhibin Wang 1, Junfei Xia 1, Peipei Zhang 1, Brett Kirkland 1, Anant K. Paravastu 1 2, Jingjiao Guan 1 3

Organizations: 1: Department of Chemical and Biomedical Engineering, FAMU-FSU College of Engineering, Florida State University, Tallahassee, FL, United States, 2: National High Magnetic Field Laboratory, Tallahassee, FL, United States, 3: Integrative NanoScience Institute, Florida State University, Tallahassee, FL, United States

Adsorption of the 40-residue Alzheimer’s β-amyloid peptide (Aβ40) on a hydrophobic surface leads to formation of potentially disease-relevant aggregates. Existing techniques are limited in characterizing the adsorbed Aβ40 and producing potentially useful Aβ40 microstructures such as microarrays and microparticles. In this paper, a novel approach based on microcontact printing (μCP) to studying and utilizing adsorption of Aβ40 monomers and fibril fragments on hydrophobic surface of polydimethylsiloxane (PDMS) stamps has been developed. By transferring the adsorbed layer from the stamp to a glass substrate, this approach allows easy measurement of thickness of the adsorbed layer. It also enables characterization of the face of the adsorbed layer in contact with the stamp surface. This face exhibits significant higher thioflavin T fluorescence than the face exposed to water, suggesting β-sheet formation induced by the PDMS surface. The intrinsic stability of the adsorbed layer is evaluated by printing the layer on a water-soluble substrate and exposing it to water vapor or water. Stable particulate microstructures in water are obtained by chemically crosslinking the adsorbed peptides. Moreover, co-micropatterning of the different states of Aβ40 (monomers and fibril fragments) is demonstrated. This μCP-based approach is simple, versatile, and holds potential for various applications.