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Imaging of amyloid-β in alzheimer’s disease transgenic mouse brains with ToF-SIMS using immunoliposomes
RISE., SP – Sveriges Tekniska Forskningsinstitut, SP Kemi Material och Ytor, Medicinteknik. Chalmers University of Technology, Sweden.
Karolinska Institute, Sweden.
Karolinska Institute, Sweden.
Karolinska Institute, Sweden.
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2016 (Engelska)Ingår i: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 11, nr 2, s. 1-11, artikel-id 02A312Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Time-of-flight secondary ion mass spectrometry (ToF-SIMS) has been proven to successfully image different kinds of molecules, especially a variety of lipids, in biological samples. Proteins, however, are difficult to detect as specific entities with this method due to extensive fragmentation. To circumvent this issue, the authors present in this work a method developed for detection of proteins using antibody-conjugated liposomes, so called immunoliposomes, which are able to bind to the specific protein of interest. In combination with the capability of ToF-SIMS to detect native lipids in tissue samples, this method opens up the opportunity to analyze many different biomolecules, both lipids and proteins, at the same time, with high spatial resolution. The method has been applied to detect and image the distribution of amyloid-β (Aβ), a biologically relevant peptide in Alzheimer’s disease (AD), in transgenic mouse brain tissue. To ensure specific binding, the immunoliposome binding was verified on a model surface using quartz crystal microbalance with dissipation monitoring. The immunoliposome binding was also investigated on tissue sections with fluorescence microscopy, and compared with conventional immunohistochemistry using primary and secondary antibodies, demonstrating specific binding to Aβ. Using ToF-SIMS imaging, several endogenous lipids, such as cholesterol and sulfatides, were also detected in parallel with the immunoliposome-labeled Aβ deposits, which is an advantage compared to fluorescence microscopy. This method can thus potentially provide further information about lipid–protein interactions, which is important to understand the mechanisms of neurodegeneration in AD.

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American Institute of Physics (AIP), 2016. Vol. 11, nr 2, s. 1-11, artikel-id 02A312
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Biofysik Biokemi och molekylärbiologi Analytisk kemi
Identifikatorer
URN: urn:nbn:se:ri:diva-27648DOI: 10.1116/1.4940215Scopus ID: 2-s2.0-85000866221OAI: oai:DiVA.org:ri-27648DiVA, id: diva2:1059498
Tillgänglig från: 2016-12-22 Skapad: 2016-12-21 Senast uppdaterad: 2023-06-05Bibliografiskt granskad

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Sjövall, Peter

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