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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| Format: | Article |
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MDPI AG
2020-11-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/23/8916 |
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| author | Kamile Mikalauskaite Mantas Ziaunys Tomas Sneideris Vytautas Smirnovas |
| author_facet | Kamile Mikalauskaite Mantas Ziaunys Tomas Sneideris Vytautas Smirnovas |
| author_sort | Kamile Mikalauskaite |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-10T14:36:27Z |
| format | Article |
| id | doaj.art-ef7bb2c52ea14255a531a44ef2eb15c2 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T14:36:27Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-ef7bb2c52ea14255a531a44ef2eb15c22023-11-20T22:11:23ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-11-012123891610.3390/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 |
| 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 |
| title | 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_short | 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 |
| topic | amyloid protein aggregation ionic strength thioflavin-T |
| url | https://www.mdpi.com/1422-0067/21/23/8916 |
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