Enhanced Fluorescent Assignment of Protein Aggregates by an Oligothiophene–Porphyrin‐Based Amyloid Ligand. Issue 9 (7th March 2013)

• Record Type: Journal Article
• Authors: Arja, Katriann; Sjölander, Daniel; Åslund, Alma; Prokop, Stefan; Heppner, Frank L.; Konradsson, Peter; Lindgren, Mikael; Hammarström, Per; Åslund, K. O. Andreas; Nilsson, K. Peter R.; Tang, B. Z.; Liu, B.
• Is Part Of: Macromolecular rapid communications. Volume 34:Issue 9(2013:May)
• Page Start: 723
• Page End: 730
• Publication Date: 2013-03-07
• Subjects: Macromolecules -- Periodicals; Polymers -- Periodicals; Chemistry -- Periodicals; 547.705
• DOI: 10.1002/marc.201200817
• Languages: English
• ISSNs: 1022-1336

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Fluorescent probes identifying protein aggregates are of great interest, as deposition of aggregated proteins is associated with many devastating diseases. Here, we report that a fluorescent amyloid ligand composed of two distinct molecular moieties, an amyloidophilic pentameric oligothiophene and a porphyrin, can be utilized for spectral and lifetime imaging assessment of recombinant Aβ 1‐42 amyloid fibrils and Aβ deposits in brain tissue sections from a transgenic mouse model with Alzheimer's disease pathology. The enhanced spectral range and distinct lifetime diversity of this novel oligothiophene–porphyrin‐based ligand allow a more precise assessment of heterogeneous amyloid morphology compared with the corresponding oligothiophene dye.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1zvgs9qx" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>