Stabilization of a metastable state of Torpedo californica acetylcholinesterase by chemical chaperones
Open accessAbstract
Chemical modification of Torpedo californica acetylcholinesterase by the natural thiosulfinate allicin produces an inactive enzyme through reaction with the buried cysteine Cys 231. Optical spectroscopy shows that the modified enzyme is “native‐like,” and inactivation can be reversed by exposure to reduced glutathione. The allicin‐modified enzyme is, however, metastable, and is converted spontaneously and irreversibly, at room temperature, with t1/2 ≃ 100 min, to a stable, partially unfolded state with the physicochemical characteristics of a molten globule. Osmolytes, including trimethylamine‐N‐oxide, glycerol, and sucrose, and the divalent cations, Ca 2+, Mg 2+, and Mn 2+ can prevent this transition of the native‐like state for >24 h at room temperature. Trimethylamine‐N‐oxide and Mg 2+ can also stabilize the native enzyme, with only slight inactivation being observed over several hours at 39°C, whereas in their absence it is totally inactivated within 5 min. The stabilizing effects of the osmolytes can be explained by their differential interaction with the native and native‐like states, resulting in a shift of equilibrium toward the native state. The stabilizing effects of the divalent cations can be ascribed to direct stabilization of the native state, as supported by differential scanning calorimetry.
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Acetylcholinesterase incubated with allicin produced rapid inactivation that was concentration- and time-dependent.
“Millard et al. [102] reported that AChE incubated with allicin produced rapid inactivation that was concentration and time-dependent.”
From Chemical Constituents and Pharmacological Activities of Garlic (Allium sativum L.): A Review (2020) · cites this paper as [102]
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- Authors
- Millard, C. B., Shnyrov, V. L., Newstead, S., Shin, I., Roth, E., Silman, I., & Weiner, L.
- Affiliations
- Weizmann Institute of Science (IL)
- Universidad de Salamanca (ES)
- Corresponding author
- Weiner, Lev
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2003-10
- Volume
- 12
- Issue
- 10
- Pages
- 2337-2347
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- PMC
- PMC2366936
- OpenAlex
- W2055769329
- Cited by
- 30
- References
- 54
- Citations by year
- 2024: 2 · 2021: 1 · 2020: 2 · 2018: 3 · 2016: 3 · 2015: 2 · 2012: 4
- FWCI
- 0.11
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Protein Science (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Israel Science Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Pharmacology › Cholinesterase and Neurodegenerative Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- Torpedo californica acetylcholinesterase, chemical chaperones, allicin, thiosulfinates, protein stabilization, metastable states, molten globule, protein unfolding, osmolytes, trimethylamine N-oxide, divalent cations, magnesium, enzyme inactivation
- MeSH terms
- Acetylcholinesterase, Algorithms, Anilino Naphthalenesulfonates, Animals, Anthracenes, Calorimetry, Differential Scanning, Catalysis, Circular Dichroism, Cross-Linking Reagents, Cysteine, Disulfides, Electrophoresis, Polyacrylamide Gel, Enzyme Inhibitors, Enzyme Stability, Glutathione, Glycerol, Hot Temperature, Hydrolysis, Kinetics, Magnesium, Methylamines, Models, Theoretical, Perylene, Protein Conformation, Protein Denaturation, Spectrometry, Fluorescence, Sulfhydryl Reagents, Sulfinic Acids, Thermodynamics, Torpedo, Trypsin
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