Behavior of α, β tubulin in DMSO-containing electrolytes. Issue 9 (6th August 2019)
- Record Type:
- Journal Article
- Title:
- Behavior of α, β tubulin in DMSO-containing electrolytes. Issue 9 (6th August 2019)
- Main Title:
- Behavior of α, β tubulin in DMSO-containing electrolytes
- Authors:
- Kalra, Aarat P.
Kar, Piyush
Preto, Jordane
Rezania, Vahid
Dogariu, Aristide
Lewis, John D.
Tuszynski, Jack A.
Shankar, Karthik - Abstract:
- Abstract : DLS and RISM are used to show that DMSO induces oligomerization in α, β tubulin dimers. DLS is thus proposed as a reliable and fast technique for the analysis of early stage microtubule kinetics. Abstract : α, β-tubulin is a cytoskeletal protein that forms cylindrical structures termed microtubules, which are crucial to the cell for a variety of roles. Microtubules are frequently modelled as one-dimensional bionanowires that act as ion transporters in the cell. In this work, we used dynamic light scattering (DLS) to measure the hydrodynamic diameter of tubulin in the presence of a polar aprotic co-solvent. We found that the hydrodynamic diameter increased with increasing DMSO volume fraction, almost doubling at 20% DMSO. To evaluate if this was due to an enlarged solvation shell, we performed reference interaction site model (RISM) simulations and found that the extent of solvation was unchanged. Using fluorescence microscopy, we then showed that tubulin was polymerization competent in the presence of colchicine, and thus inferred the presence of oligomers in the presence of DMSO, which points to its mechanism of action as a microtubule polymerization enhancing agent. Tubulin oligomers are known to form when microtubules depolymerize and are controversially implicated in microtubule polymerization. We show that DLS may be used to monitor early-state microtubule polymerization and is a viable alternative to fluorescence and electron microscopy-based methods. OurAbstract : DLS and RISM are used to show that DMSO induces oligomerization in α, β tubulin dimers. DLS is thus proposed as a reliable and fast technique for the analysis of early stage microtubule kinetics. Abstract : α, β-tubulin is a cytoskeletal protein that forms cylindrical structures termed microtubules, which are crucial to the cell for a variety of roles. Microtubules are frequently modelled as one-dimensional bionanowires that act as ion transporters in the cell. In this work, we used dynamic light scattering (DLS) to measure the hydrodynamic diameter of tubulin in the presence of a polar aprotic co-solvent. We found that the hydrodynamic diameter increased with increasing DMSO volume fraction, almost doubling at 20% DMSO. To evaluate if this was due to an enlarged solvation shell, we performed reference interaction site model (RISM) simulations and found that the extent of solvation was unchanged. Using fluorescence microscopy, we then showed that tubulin was polymerization competent in the presence of colchicine, and thus inferred the presence of oligomers in the presence of DMSO, which points to its mechanism of action as a microtubule polymerization enhancing agent. Tubulin oligomers are known to form when microtubules depolymerize and are controversially implicated in microtubule polymerization. We show that DLS may be used to monitor early-state microtubule polymerization and is a viable alternative to fluorescence and electron microscopy-based methods. Our findings showing that DMSO causes tubulin oligomerization are thus of critical importance, both for creating bio-inspired nanotechnology and determining its biophysical roles in the cell. … (more)
- Is Part Of:
- Nanoscale advances. Volume 1:Issue 9(2019)
- Journal:
- Nanoscale advances
- Issue:
- Volume 1:Issue 9(2019)
- Issue Display:
- Volume 1, Issue 9 (2019)
- Year:
- 2019
- Volume:
- 1
- Issue:
- 9
- Issue Sort Value:
- 2019-0001-0009-0000
- Page Start:
- 3364
- Page End:
- 3371
- Publication Date:
- 2019-08-06
- Subjects:
- 620.5
- Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/na#!recentarticles&adv ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c9na00035f ↗
- Languages:
- English
- ISSNs:
- 2516-0230
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 12664.xml