Fluorescence correlation spectroscopy measurements on amyloid fibril reveal at least two binding modes for fluorescent sensors
Interaction of fluorophore with amyloid structure is central to the design and development of fluorescent sensors. In literature ensemble spectroscopy results reveal at least two distinct binding modes for most of the torsional probes like Thioflavin-T, SYPRO Orange, etc. though single molecule loca...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-12-01
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| Series: | Chemical Physics Impact |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667022423002086 |
| _version_ | 1797400863783780352 |
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| author | Aranyak Sarkar Vinu Namboodiri Manoj Kumbhakar |
| author_facet | Aranyak Sarkar Vinu Namboodiri Manoj Kumbhakar |
| author_sort | Aranyak Sarkar |
| collection | DOAJ |
| description | Interaction of fluorophore with amyloid structure is central to the design and development of fluorescent sensors. In literature ensemble spectroscopy results reveal at least two distinct binding modes for most of the torsional probes like Thioflavin-T, SYPRO Orange, etc. though single molecule localization microscopy and spectroscopy results consider only one binding mode. To address this discrepancy we employed fluorescence correlation spectroscopy (FCS) to measure the binding kinetics on immobilized fibril structures with single molecule sensitivity. Our results indicate that there are at least two possible biding configurations with differing relaxation time constants indicating possible weaker and stronger binding configurations depending on the local environment on the fibril structure. Critical evaluation of on-time distributions from the recorded wide-field image stack for single molecule localization microscopy image, further highlight the presence of two burst times. Such bi-modal binding behavior is attributed to the differing binding configurations on fibril architecture. |
| first_indexed | 2024-03-09T02:00:39Z |
| format | Article |
| id | doaj.art-5d7a24687b0f429d85950c2fcf23231d |
| institution | Directory Open Access Journal |
| issn | 2667-0224 |
| language | English |
| last_indexed | 2024-03-09T02:00:39Z |
| publishDate | 2023-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Chemical Physics Impact |
| spelling | doaj.art-5d7a24687b0f429d85950c2fcf23231d2023-12-08T04:46:48ZengElsevierChemical Physics Impact2667-02242023-12-017100369Fluorescence correlation spectroscopy measurements on amyloid fibril reveal at least two binding modes for fluorescent sensorsAranyak Sarkar0Vinu Namboodiri1Manoj Kumbhakar2Radiation & Photochemistry Division, Bhabha Atomic Research Center, Mumbai 400085, India; Homi Bhabha National Institute, Training School Complex, Anushaktinagar, Mumbai 400094, IndiaRadiation & Photochemistry Division, Bhabha Atomic Research Center, Mumbai 400085, IndiaRadiation & Photochemistry Division, Bhabha Atomic Research Center, Mumbai 400085, India; Homi Bhabha National Institute, Training School Complex, Anushaktinagar, Mumbai 400094, India; Corresponding author.Interaction of fluorophore with amyloid structure is central to the design and development of fluorescent sensors. In literature ensemble spectroscopy results reveal at least two distinct binding modes for most of the torsional probes like Thioflavin-T, SYPRO Orange, etc. though single molecule localization microscopy and spectroscopy results consider only one binding mode. To address this discrepancy we employed fluorescence correlation spectroscopy (FCS) to measure the binding kinetics on immobilized fibril structures with single molecule sensitivity. Our results indicate that there are at least two possible biding configurations with differing relaxation time constants indicating possible weaker and stronger binding configurations depending on the local environment on the fibril structure. Critical evaluation of on-time distributions from the recorded wide-field image stack for single molecule localization microscopy image, further highlight the presence of two burst times. Such bi-modal binding behavior is attributed to the differing binding configurations on fibril architecture.http://www.sciencedirect.com/science/article/pii/S2667022423002086Transient amyloid blinkingSuper resolution imagingMolecular rotorHydrophobic probesSensor binding |
| spellingShingle | Aranyak Sarkar Vinu Namboodiri Manoj Kumbhakar Fluorescence correlation spectroscopy measurements on amyloid fibril reveal at least two binding modes for fluorescent sensors Chemical Physics Impact Transient amyloid blinking Super resolution imaging Molecular rotor Hydrophobic probes Sensor binding |
| title | Fluorescence correlation spectroscopy measurements on amyloid fibril reveal at least two binding modes for fluorescent sensors |
| title_full | Fluorescence correlation spectroscopy measurements on amyloid fibril reveal at least two binding modes for fluorescent sensors |
| title_fullStr | Fluorescence correlation spectroscopy measurements on amyloid fibril reveal at least two binding modes for fluorescent sensors |
| title_full_unstemmed | Fluorescence correlation spectroscopy measurements on amyloid fibril reveal at least two binding modes for fluorescent sensors |
| title_short | Fluorescence correlation spectroscopy measurements on amyloid fibril reveal at least two binding modes for fluorescent sensors |
| title_sort | fluorescence correlation spectroscopy measurements on amyloid fibril reveal at least two binding modes for fluorescent sensors |
| topic | Transient amyloid blinking Super resolution imaging Molecular rotor Hydrophobic probes Sensor binding |
| url | http://www.sciencedirect.com/science/article/pii/S2667022423002086 |
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