Computational predictions of volatile anesthetic interactions with the microtubule cytoskeleton: implications for side effects of general anesthesia
Open accessAbstract
The cytoskeleton is essential to cell morphology, cargo trafficking, and cell division. As the neuronal cytoskeleton is extremely complex, it is no wonder that a startling number of neurodegenerative disorders (including but not limited to Alzheimer's disease, Parkinson's disease and Huntington's disease) share the common feature of a dysfunctional neuronal cytoskeleton. Recently, concern has been raised about a possible link between anesthesia, post-operative cognitive dysfunction, and the exacerbation of neurodegenerative disorders. Experimental investigations suggest that anesthetics bind to and affect cytoskeletal microtubules, and that anesthesia-related cognitive dysfunction involves microtubule instability, hyper-phosphorylation of the microtubule-associated protein tau, and tau separation from microtubules. However, exact mechanisms are yet to be identified. In this paper the interaction of anesthetics with the microtubule subunit protein tubulin is investigated using computer-modeling methods. Homology modeling, molecular dynamics simulations and surface geometry techniques were used to determine putative binding sites for volatile anesthetics on tubulin. This was followed by free energy based docking calculations for halothane (2-bromo-2-chloro-1,1,1-trifluoroethane) on the tubulin body, and C-terminal regions for specific tubulin isotypes. Locations of the putative binding sites, halothane binding energies and the relation to cytoskeleton function are reported in this paper.
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Tubulin contains 32 aromatic (phenyl and indole) amino acid rings with π electron resonance clouds, most within a Forster resonance transfer distance of 1 to 2 nanometers.
“Tubulin (Fig. 5) contains 32 aromatic (phenyl and indole) amino acid rings with π electron resonance clouds, most within a Forster resonance transfer distance of 1 to 2 nanometers [79].”
From Consciousness in the universe (2014) · cites this paper as [79]
The Discussion section, “Comparison to Aromatic Amino Acids” (page unavailable), reports 43 phenylalanine and 8 tryptophan residues in tubulin, contrary to the claimed total of 32 phenyl and indole rings. The paper’s figure of 32 refers instead to predicted anesthetic-binding sites (“Interaction Mechanisms”). Our copy does not establish that most aromatic rings are within a 1–2 nm Förster transfer distance. (LLM, conf=0.86)
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- Authors
- Craddock, T. J. A., St. George, M., Freedman, H., Barakat, K. H., Damaraju, S., Hameroff, S., & Tuszynski, J. A.
- Affiliations
- University of Alberta (CA)
- University of Algarve (PT)
- University of Arizona (US)
- Corresponding author
- Craddock, Travis J. A.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-06-25
- Volume
- 7
- Issue
- 6
- Pages
- e37251
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3382613
- OpenAlex
- W2034360520
- Cited by
- 84
- References
- 118
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 1 · 2023: 6 · 2022: 15 · 2021: 3 · 2020: 3 · 2019: 3 · 2018: 5 · 2017: 7 · 2016: 9 · 2015: 7 · 2014: 8 · 2013: 8 · 2012: 1
- FWCI
- 2.58
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- NSUWorks (Nova Southeastern University) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, cc-by)
- Funders
- Ministry of Advanced Education, Government of Alberta
- Alberta Cancer Foundation
- Allard Foundation
- Natural Sciences and Engineering Research Council of Canada
- Fundação para a Ciência e a Tecnologia
- Topics
- Life Sciences › Neuroscience › Developmental Neuroscience › Anesthesia and Neurotoxicity Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Physical Sciences › Computer Science › Computational Theory and Mathematics › Computational Drug Discovery Methods
- Keywords
- volatile anesthetics, microtubules, tubulin, halothane, anesthetic binding sites, postoperative cognitive dysfunction, neurodegenerative diseases, tau hyperphosphorylation, microtubule instability, anesthetic side effects
- MeSH terms
- Anesthesia, General, Anesthetics, Computer Simulation, Cytoskeleton, Halothane, Humans, Microtubules, Models, Chemical, Protein Conformation, Tubulin, Volatilization, Neurodegenerative Diseases
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