Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity
The formation of amyloid fibrils is linked to multiple neurodegenerative disorders, including Alzheimer’s and Parkinson’s disease. Despite years of research and countless studies on the topic of such aggregate formation, as well as their resulting structure, the current knowledge is still fairly lim...
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doaj-ef7bb2c52ea14255a531a44ef2eb15c22020-11-27T07:57:14ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-11-01218916891610.3390/ijms21238916Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence IntensityKamile Mikalauskaite0Mantas Ziaunys1Tomas Sneideris2Vytautas Smirnovas3Institute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaInstitute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaInstitute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaInstitute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaThe formation of amyloid fibrils is linked to multiple neurodegenerative disorders, including Alzheimer’s and Parkinson’s disease. Despite years of research and countless studies on the topic of such aggregate formation, as well as their resulting structure, the current knowledge is still fairly limited. One of the main aspects prohibiting effective aggregation tracking is the environment’s effect on amyloid-specific dyes, namely thioflavin-T (ThT). Currently, there are only a few studies hinting at ionic strength being one of the factors that modulate the dye’s binding affinity and fluorescence intensity. In this work we explore this effect under a range of ionic strength conditions, using insulin, lysozyme, mouse prion protein, and α-synuclein fibrils. We show that ionic strength is an extremely important factor affecting both the binding affinity, as well as the fluorescence intensity of ThT.https://www.mdpi.com/1422-0067/21/23/8916amyloidprotein aggregationionic strengththioflavin-T |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Kamile Mikalauskaite Mantas Ziaunys Tomas Sneideris Vytautas Smirnovas |
spellingShingle |
Kamile Mikalauskaite Mantas Ziaunys Tomas Sneideris Vytautas Smirnovas Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity International Journal of Molecular Sciences amyloid protein aggregation ionic strength thioflavin-T |
author_facet |
Kamile Mikalauskaite Mantas Ziaunys Tomas Sneideris Vytautas Smirnovas |
author_sort |
Kamile Mikalauskaite |
title |
Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity |
title_short |
Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity |
title_full |
Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity |
title_fullStr |
Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity |
title_full_unstemmed |
Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity |
title_sort |
effect of ionic strength on thioflavin-t affinity to amyloid fibrils and its fluorescence intensity |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2020-11-01 |
description |
The formation of amyloid fibrils is linked to multiple neurodegenerative disorders, including Alzheimer’s and Parkinson’s disease. Despite years of research and countless studies on the topic of such aggregate formation, as well as their resulting structure, the current knowledge is still fairly limited. One of the main aspects prohibiting effective aggregation tracking is the environment’s effect on amyloid-specific dyes, namely thioflavin-T (ThT). Currently, there are only a few studies hinting at ionic strength being one of the factors that modulate the dye’s binding affinity and fluorescence intensity. In this work we explore this effect under a range of ionic strength conditions, using insulin, lysozyme, mouse prion protein, and α-synuclein fibrils. We show that ionic strength is an extremely important factor affecting both the binding affinity, as well as the fluorescence intensity of ThT. |
topic |
amyloid protein aggregation ionic strength thioflavin-T |
url |
https://www.mdpi.com/1422-0067/21/23/8916 |
work_keys_str_mv |
AT kamilemikalauskaite effectofionicstrengthonthioflavintaffinitytoamyloidfibrilsanditsfluorescenceintensity AT mantasziaunys effectofionicstrengthonthioflavintaffinitytoamyloidfibrilsanditsfluorescenceintensity AT tomassneideris effectofionicstrengthonthioflavintaffinitytoamyloidfibrilsanditsfluorescenceintensity AT vytautassmirnovas effectofionicstrengthonthioflavintaffinitytoamyloidfibrilsanditsfluorescenceintensity |
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1724414087090143232 |