Proteophenes - Amino Acid Functionalized Thiophene-based Fluorescent Ligands for Visualization of Protein Deposits in Tissue Sections with Alzheimer's Disease Pathology.
Proteophenes - Amino Acid Functionalized Thiophene-based Fluorescent Ligands for Visualization of Protein Deposits in Tissue Sections with Alzheimer's Disease Pathology.
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DOI：
10.1002/chem.202201557
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发表时间：
2022-11-07
影响因子：
4.3
通讯作者：
Nilsson, K. Peter R.
中科院分区：
文献类型：
--
作者：
Bjork, Linnea;Back, Marcus;Lantz, Linda;Ghetti, Bernardino;Vidal, Ruben;Klingstedt, Therese;Nilsson, K. Peter R.
Protein deposits composed of specific proteins or peptides are associated with several neurodegenerative diseases and fluorescent ligands able to detect these pathological hallmarks are vital. Here, we report the synthesis of a class of thiophene‐based ligands, denoted proteophenes, with different amino acid side‐chain functionalities along the conjugated backbone, which display selectivity towards specific disease‐associated protein aggregates in tissue sections with Alzheimer's disease (AD) pathology. The selectivity of the ligands towards AD associated pathological hallmarks, such as aggregates of the amyloid‐β (Aβ) peptide or tau filamentous inclusions, was highly dependent on the chemical nature of the amino acid functionality, as well as on the location of the functionality along the pentameric thiophene backbone. Finally, the concept of synthesizing donor‐acceptor‐donor proteophenes with distinct photophysical properties was shown. Our findings provide the structural and functional basis for the development of new thiophene‐based ligands that can be utilized for optical assignment of different aggregated proteinaceous species in tissue sections. Proteophenes. A palette of fluorescent thiophene‐based ligands with distinct amino acid side‐chain functionalities along the conjugated backbone was synthesized. Ligands with specific side‐chain functionalities displayed selectivity towards distinct protein aggregates in tissue sections with Alzheimer's disease pathology. We foresee that proteophenes will significantly expand the toolbox of ligands for fluorescent assignment of disease‐associated protein aggregates.
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影响因子：
15.1
作者：
Barth M;Bacioglu M;Schwarz N;Novotny R;Brandes J;Welzer M;Mazzitelli S;Häsler LM;Schweighauser M;Wuttke TV;Kronenberg-Versteeg D;Fog K;Ambjørn M;Alik A;Melki R;Kahle PJ;Shimshek DR;Koch H;Jucker M;Tanriöver G
通讯作者：
Tanriöver G
影响因子：
3.2
作者：
Klingstedt T;Aslund A;Simon RA;Johansson LB;Mason JJ;Nyström S;Hammarström P;Nilsson KP
通讯作者：
Nilsson KP
由硫烯基淀粉样蛋白配体染色的Prion菌株特异性PRP沉积物的多模式荧光显微镜。
影响因子：
2.3
作者：
Magnusson K;Simon R;Sjölander D;Sigurdson CJ;Hammarström P;Nilsson KP
通讯作者：
Nilsson KP
DOI：
10.1002/cphc.202000669
发表时间：
2021-02-03
期刊：
Chemphyschem : a European journal of chemical physics and physical chemistry
影响因子：
--
作者：
Gustafsson C;Shirani H;Leira P;Rehn DR;Linares M;Nilsson KPR;Norman P;Lindgren M
通讯作者：
Lindgren M
影响因子：
17.1
作者：
Herrmann, Uli S.;Schuetz, Anne K.;Aguzzi, Adriano
通讯作者：
Aguzzi, Adriano