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September 14, 2026 at 9:49 PM
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EFTA00606068 | EFTA00606072 sites of the various anesthetics on tubulin. On average, the preference for anesthetics to bind at a tubulin site are ordered as site 7, 5, 38, 4, 1, 23, 37, and finally 21. However, statistical difference (p < 0.05) was only found between site 21 and sites 4, 5, 7 and 38. No other significant differences were found, suggesting that there is no overall preferred binding site for anesthetics to tubulin. Still, it is worth noting that sites 7 and 38 are within 5 angstroms of key residues of the colchicine-binding pocket which is consistent with the volatile anesthetic halothane being shown to reduce colchicine binding to tubulini9. Furthermore, sites 5, 7, and 38 are all within 5 angstroms of residues that interact with either the intradimer non-exchangeable GTP molecule or the magnesium ion required for the intradimer alpha-beta tubulin stability, and may be a mechanism by which volatile anesthetics disrupt microtubule structureS0. Quantum Chemical Estimate of Polarizability and MAC. We calculated the mean polarizability and polarizability tensors for all It agents listed in Fig. 1 using a density functional theory approach. The results of our quantum chemical estimate of mean polarizability are shown in Fig. 2B and listed in Table SI, along with experimental measures of anesthetic MAC and predicted MAC for non-anesthetics and convulsants. However, these estimates are based on the mean polarizabilities of the molecules and does not account for the directions of polarization, permanent dipole moments, or docking orientation of agents to a given protein. To investigate the full effect of anesthetic, non-anesthetic, and convulsant polarizabilities and permanent dipole moments on the collective electronic behavior of the tubulin dimer, we calculated the molecular dipole components induced by London dispersion forces between the highly polarizable aromatic amino acids tryptophan, tyrosine, and phenylalanine based on their molecular polarizability tensors, and evaluated the change between collective dipole oscillations in the presence and absence of the agent molecules. In the absence ofagent molecules the aromatic amino acids of tubulin set up normal oscillatory modes that range in frequency between 480 and 700 THz (1THz = 1012 Hz). This result provides a first-order description of the collective oscillation in tubulin. A full quantum mechanical parametrization of the coupled atomic dipolar fluctuations in valence electronic response, as done in the many-body dispersion approach to describe collective wavelike charge density fluctuations", would provide a more refined estimate of this behavior. The presence of an agent molecule creates another normal mode of dipole oscillation for the aromatic-agent network In Fig. 3 we plot these new normal modes created by the addition ofan agent as a function of their MAC. A clear polynomial trend can be seen for anesthetics alone, with a very high degree of correlation (R.2= 0.995), which is slightly greater than that found for the Meyer-Overton relation (Fig. 2A). While the anesthetidconvulsant tlurothyl also follows this trend, the non-anesthetics both do not. Rather, due to the polynomial nature of the relation the minimum possible frequency that would lie on the curve is 594 THz, which is marginally greater than both of the frequencies introduced by the non-anesthetics investigated, suggesting the non-anesthetics fall below a cutoffrequired for anesthetic action. The biological importance of this range is not fully understood at this time. The introduction of an agent also shifts the normal oscillatory modes of the aromatic dipoles by an order of to 100 GHz (1GHz = 10°Hz). Figure 4A shows specific plots illustrating the shifts in the oscillation frequencies of tubulin's aromatic amino acids for agents docked at each of the predicted tubulin binding sites. No correlation between peak shift in frequency and binding site energy was found. The most prominent shift observed for all the anesthetic agents was observed as a decrease in the normal mode of oscillation in the range of (613 ± 8) THz. Both the biological significance of this range and the relevance of a decrease in oscillation frequency to anesthetic action, versus an increase, require further investigation. The maximum frequency decrease in this range induced by anesthetics correlates with MAC (R2= 0.999) (Fig. 4B). Flurothyl again followed the same trend as the anesthetics, while F6 and TFMB did not show any decreases in this range, but rather showed increases in oscillation frequency. Of note is that the predicted MAC of the non-anesthetics is greater than 1000% atm well beyond physiologically relevant concentrations, correctly predicting their lack of anesthetic action. Discussion Anesthesia is one of the great achievements of modern medicine, yet the mechanisms by which anesthetics selectively block consciousness and memory formation, while sparing non-conscious brain activities, remain unclear in spite of a century and a half of clinical use. Understanding anesthetic mechanisms may shed light on several problems in consciousness studies, which would be an important scientific and philosophical achievement. More practically, a better understanding of anesthesia can aid in clinical decisions to reduce the risk of adverse effects including POCD, particularly in those suffering from neurodegenerative conditions, and/or lead to the rational design and development of anesthetics with fewer deleterious side effects. Yet how do anesthetic gases, a disparate group of volatile chemical compounds, exert a common, unitary effect in all animals at concentrations specific to each gas? The Meyer-Overton correlation implies a unifying factor related to the solubility of a gas in lipid-like, non-polar hydrophobic solvents. Binding in these solvents occurs by very weak London dipole dispersion, a type of weak van der Waals force, but the significance of the Meyer-Overton correlation remains elusive. Solubility in lipids alone does not account for the cut-off' effect2azs anesthetic differences due to chirality", the lack of other lipid-altering effects to cause anesthesia", or the role of membrane proteins in neuron excitability, leading to the conclusion that anesthetics act in non-polar, hydrophobic regions within proteins. Furthermore, there are exceptions to the Meyer-Overton rule where an agent's lipid solubility predicts it to have a significant anesthetic potency, but it does not (i.e. P6, TFMB). These exceptions, however, may provide insight into the mechanisms of anesthetics. Examining how molecular polarizability correlates with anesthetic potency reveals a discontinuity with the Meyer-Overton rule, specifically for the non-anesthetics F6 and TFMB. What is the difference in relation between non-polar, 'lipid' solubility and polarizability such that these gases don't cause anesthesia? In this paper we investigate this relationship and present a computational study aimed at examining the effect ofanesthetic, non-anesthetic, and anesthetic/convulsant agent polarizabilities and permanent dipole moments on protein function. SCIENTIFIC RE PORTS17: 9877 IDOI:181038N41598-017-09992-7 5 EFTA00606072
May 4, 2026 at 1:08 PM