Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions
The functional structure of proteins results from marginally stable folded conformations. Reversible unfolding, irreversible denaturation, and deterioration can be caused by chemical and physical agents due to changes in the physicochemical conditions of pH, ionic strength, temperature, pressure, an...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-10-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/27/20/6861 |
| _version_ | 1797470911442452480 |
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| author | Patrick Masson Sofya Lushchekina |
| author_facet | Patrick Masson Sofya Lushchekina |
| author_sort | Patrick Masson |
| collection | DOAJ |
| description | The functional structure of proteins results from marginally stable folded conformations. Reversible unfolding, irreversible denaturation, and deterioration can be caused by chemical and physical agents due to changes in the physicochemical conditions of pH, ionic strength, temperature, pressure, and electric field or due to the presence of a cosolvent that perturbs the delicate balance between stabilizing and destabilizing interactions and eventually induces chemical modifications. For most proteins, denaturation is a complex process involving transient intermediates in several reversible and eventually irreversible steps. Knowledge of protein stability and denaturation processes is mandatory for the development of enzymes as industrial catalysts, biopharmaceuticals, analytical and medical bioreagents, and safe industrial food. Electrophoresis techniques operating under extreme conditions are convenient tools for analyzing unfolding transitions, trapping transient intermediates, and gaining insight into the mechanisms of denaturation processes. Moreover, quantitative analysis of electrophoretic mobility transition curves allows the estimation of the conformational stability of proteins. These approaches include polyacrylamide gel electrophoresis and capillary zone electrophoresis under cold, heat, and hydrostatic pressure and in the presence of non-ionic denaturing agents or stabilizers such as polyols and heavy water. Lastly, after exposure to extremes of physical conditions, electrophoresis under standard conditions provides information on irreversible processes, slow conformational drifts, and slow renaturation processes. The impressive developments of enzyme technology with multiple applications in fine chemistry, biopharmaceutics, and nanomedicine prompted us to revisit the potentialities of these electrophoretic approaches. This feature review is illustrated with published and unpublished results obtained by the authors on cholinesterases and paraoxonase, two physiologically and toxicologically important enzymes. |
| first_indexed | 2024-03-09T19:42:39Z |
| format | Article |
| id | doaj.art-aa8121ffff1544bf95b31950c9003981 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T19:42:39Z |
| publishDate | 2022-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-aa8121ffff1544bf95b31950c90039812023-11-24T01:32:32ZengMDPI AGMolecules1420-30492022-10-012720686110.3390/molecules27206861Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme ConditionsPatrick Masson0Sofya Lushchekina1Biochemical Neuropharmacology Laboratory, Kazan Federal University, Kremlievskaya Str. 18, 420111 Kazan, RussiaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Kosygin Str. 4, 119334 Moscow, RussiaThe functional structure of proteins results from marginally stable folded conformations. Reversible unfolding, irreversible denaturation, and deterioration can be caused by chemical and physical agents due to changes in the physicochemical conditions of pH, ionic strength, temperature, pressure, and electric field or due to the presence of a cosolvent that perturbs the delicate balance between stabilizing and destabilizing interactions and eventually induces chemical modifications. For most proteins, denaturation is a complex process involving transient intermediates in several reversible and eventually irreversible steps. Knowledge of protein stability and denaturation processes is mandatory for the development of enzymes as industrial catalysts, biopharmaceuticals, analytical and medical bioreagents, and safe industrial food. Electrophoresis techniques operating under extreme conditions are convenient tools for analyzing unfolding transitions, trapping transient intermediates, and gaining insight into the mechanisms of denaturation processes. Moreover, quantitative analysis of electrophoretic mobility transition curves allows the estimation of the conformational stability of proteins. These approaches include polyacrylamide gel electrophoresis and capillary zone electrophoresis under cold, heat, and hydrostatic pressure and in the presence of non-ionic denaturing agents or stabilizers such as polyols and heavy water. Lastly, after exposure to extremes of physical conditions, electrophoresis under standard conditions provides information on irreversible processes, slow conformational drifts, and slow renaturation processes. The impressive developments of enzyme technology with multiple applications in fine chemistry, biopharmaceutics, and nanomedicine prompted us to revisit the potentialities of these electrophoretic approaches. This feature review is illustrated with published and unpublished results obtained by the authors on cholinesterases and paraoxonase, two physiologically and toxicologically important enzymes.https://www.mdpi.com/1420-3049/27/20/6861gel electrophoresiscapillary electrophoresisprotein denaturationunfoldingrefoldingstability |
| spellingShingle | Patrick Masson Sofya Lushchekina Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions Molecules gel electrophoresis capillary electrophoresis protein denaturation unfolding refolding stability |
| title | Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions |
| title_full | Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions |
| title_fullStr | Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions |
| title_full_unstemmed | Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions |
| title_short | Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions |
| title_sort | conformational stability and denaturation processes of proteins investigated by electrophoresis under extreme conditions |
| topic | gel electrophoresis capillary electrophoresis protein denaturation unfolding refolding stability |
| url | https://www.mdpi.com/1420-3049/27/20/6861 |
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