Deciphering the Electronic Transitions of Thiophene-Based Donor-Acceptor-Donor Pentameric Ligands Utilized for Multimodal Fluorescence Microscopy of Protein Aggregates.

Deciphering the Electronic Transitions of Thiophene-Based Donor-Acceptor-Donor Pentameric Ligands Utilized for Multimodal Fluorescence Microscopy of Protein Aggregates.
复制标题

DOI:
10.1002/cphc.202000669
复制
发表时间:
2021-02-03
期刊:
Chemphyschem : a European journal of chemical physics and physical chemistry
影响因子:
--
通讯作者:
Lindgren M
Lindgren M
中科院分区:
其他
文献类型:
--
作者:
Gustafsson C;Shirani H;Leira P;Rehn DR;Linares M;Nilsson KPR;Norman P;Lindgren M

文献摘要

参考文献

被引文献

相似文献

Anionic pentameric thiophene acetates can be used for fluorescence detection and diagnosis of protein amyloid aggregates. Replacing the central thiophene unit by benzothiadiazole (BTD) or quinoxaline (QX) leads to large emission shifts and basic spectral features have been reported [Chem. Eur. J. 2015, 21, 15133‐13137]. Here we present new detailed experimental results of solvent effects, time‐resolved fluorescence and examples employing multi‐photon microscopy and lifetime imaging. Quantum chemical response calculations elucidate how the introduction of the BTD/QX groups changes the electronic states and emissions. The dramatic red‐shift follows an increased conjugation and quinoid character of the π‐electrons of the thiophene backbone. An efficient charge transfer in the excited states S1 and S2 compared to the all‐thiophene analogue makes these more sensitive to the polarity and quenching by the solvent. Taken together, the results guide in the interpretation of images of stained Alzheimer disease brain sections employing advanced fluorescence microscopy and lifetime imaging, and can aid in optimizing future fluorescent ligand development. Fluorescent biomarkers: The introduction of donor‐acceptor‐donor moieties in luminescent conjugated oligothiophenes gives a drastic shift in spectroscopic profile. This opens up for designing novel fluorescent biomarkers that can classify different types of amyloid folds and differentiate different morphological protein topologies.
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。
DOI: 10.4161/pri.29239
发表时间: 2014
期刊: Prion
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: 10.1039/df9500900014
发表时间: 1950-01-01
期刊: DISCUSSIONS OF THE FARADAY SOCIETY
影响因子: --
作者:
KASHA, M
通讯作者: KASHA, M
DOI: 10.1016/s0006-3495(02)75666-x
发表时间: 2002-06-01
影响因子: 3.4
作者:
Cioni, P;Strambini, GB
通讯作者: Strambini, GB
DOI: 10.1111/bpa.12598
发表时间: 2018-11-01
期刊: BRAIN PATHOLOGY
影响因子: 6.4
作者:
Aguilar-Calvo, Patricia;Bett, Cyrus;Sigurdson, Christina J.
通讯作者: Sigurdson, Christina J.
DOI: 10.1021/cb900112v
发表时间: 2009-08-21
影响因子: 4
作者:
Aslund, Andreas;Sigurdson, Christina J.;Klingstedt, Therese;Grathwohl, Stefan;Bolmont, Tristan;Dickstein, Dara L.;Glimsdal, Eirik;Prokop, Stefan;Lindgren, Mikael;Konradsson, Peter;Holtzman, David M.;Hof, Patrick R.;Heppner, Frank L.;Gandy, Samuel;Jucker, Mathias;Aguzzi, Adriano;Hammarstrom, Per;Nilsson, K. Peter R.
通讯作者: Nilsson, K. Peter R.