Rationalizing the Role of Monosodium Glutamate in the Protein Aggregation Through Biophysical Approaches: Potential Impact on Neurodegeneration
Monosodium glutamate (MSG) is the world’s most extensively used food additive and is generally recognized as safe according to the FDA. However, it is well reported that MSG is associated with a number of neurological diseases, and in turn, neurological diseases are associated with protein aggregati...
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| Format: | Article |
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Frontiers Media S.A.
2021-03-01
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| Series: | Frontiers in Neuroscience |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fnins.2021.636454/full |
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| author | Ishfaq Ahmad Ahanger Ishfaq Ahmad Ahanger Sania Bashir Zahoor Ahmad Parray Mohamed F. Alajmi Afzal Hussain Faizan Ahmad Md. Imtaiyaz Hassan Asimul Islam Anurag Sharma |
| author_facet | Ishfaq Ahmad Ahanger Ishfaq Ahmad Ahanger Sania Bashir Zahoor Ahmad Parray Mohamed F. Alajmi Afzal Hussain Faizan Ahmad Md. Imtaiyaz Hassan Asimul Islam Anurag Sharma |
| author_sort | Ishfaq Ahmad Ahanger |
| collection | DOAJ |
| description | Monosodium glutamate (MSG) is the world’s most extensively used food additive and is generally recognized as safe according to the FDA. However, it is well reported that MSG is associated with a number of neurological diseases, and in turn, neurological diseases are associated with protein aggregation. This study rationalized the role of MSG in protein aggregation using different biophysical techniques such as absorption, far-UV CD, DLS, and ITC. Kinetic measurements revealed that MSG causes significant enhancement of aggregation of BSA through a nucleation-dependent polymerization mechanism. Also, CTAB-BSA aggregation is enhanced by MSG significantly. MSG-induced BSA aggregation also exhibits the formation of irreversible aggregates, temperature dependence, non-Arrhenius behavior, and enhancement of hydrodynamic diameter. From the isothermal titration calorimetry measurement, the significant endothermic heat of the interaction of BSA-MSG indicates that protein aggregation may be due to the coupling of MSG with the protein. The determined enthalpy change (ΔH) is largely positive, also suggesting an endothermic nature, whereas entropy change (ΔS) is positive and Gibbs free energy change (ΔG) is largely negative, suggesting the spontaneous nature of the interaction. Furthermore, even a low concentration of MSG is involved in the unfolding of the secondary structure of protein with the disappearance of original peaks and the formation of a unique peak in the far-UV CD, which is an attention-grabbing observation. This is the first investigation which links the dietary MSG with protein aggregation and thus will be very instrumental in understanding the mechanism of various MSG-related human physiological as well as neurological diseases. |
| first_indexed | 2024-12-13T23:24:29Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 1662-453X |
| language | English |
| last_indexed | 2024-12-13T23:24:29Z |
| publishDate | 2021-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Neuroscience |
| spelling | doaj.art-9c25770785694e66b161e6dac24bd6fb2022-12-21T23:27:36ZengFrontiers Media S.A.Frontiers in Neuroscience1662-453X2021-03-011510.3389/fnins.2021.636454636454Rationalizing the Role of Monosodium Glutamate in the Protein Aggregation Through Biophysical Approaches: Potential Impact on NeurodegenerationIshfaq Ahmad Ahanger0Ishfaq Ahmad Ahanger1Sania Bashir2Zahoor Ahmad Parray3Mohamed F. Alajmi4Afzal Hussain5Faizan Ahmad6Md. Imtaiyaz Hassan7Asimul Islam8Anurag Sharma9Department of Chemistry, Biochemistry and Forensic Science, Amity School of Applied Sciences, Amity University Haryana, Gurgaon, IndiaCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, IndiaCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, IndiaCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, IndiaDepartment of Pharmacognosy College of Pharmacy, King Saud University, Riyadh, Saudi ArabiaDepartment of Pharmacognosy College of Pharmacy, King Saud University, Riyadh, Saudi ArabiaCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, IndiaCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, IndiaCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, IndiaDepartment of Chemistry, Biochemistry and Forensic Science, Amity School of Applied Sciences, Amity University Haryana, Gurgaon, IndiaMonosodium glutamate (MSG) is the world’s most extensively used food additive and is generally recognized as safe according to the FDA. However, it is well reported that MSG is associated with a number of neurological diseases, and in turn, neurological diseases are associated with protein aggregation. This study rationalized the role of MSG in protein aggregation using different biophysical techniques such as absorption, far-UV CD, DLS, and ITC. Kinetic measurements revealed that MSG causes significant enhancement of aggregation of BSA through a nucleation-dependent polymerization mechanism. Also, CTAB-BSA aggregation is enhanced by MSG significantly. MSG-induced BSA aggregation also exhibits the formation of irreversible aggregates, temperature dependence, non-Arrhenius behavior, and enhancement of hydrodynamic diameter. From the isothermal titration calorimetry measurement, the significant endothermic heat of the interaction of BSA-MSG indicates that protein aggregation may be due to the coupling of MSG with the protein. The determined enthalpy change (ΔH) is largely positive, also suggesting an endothermic nature, whereas entropy change (ΔS) is positive and Gibbs free energy change (ΔG) is largely negative, suggesting the spontaneous nature of the interaction. Furthermore, even a low concentration of MSG is involved in the unfolding of the secondary structure of protein with the disappearance of original peaks and the formation of a unique peak in the far-UV CD, which is an attention-grabbing observation. This is the first investigation which links the dietary MSG with protein aggregation and thus will be very instrumental in understanding the mechanism of various MSG-related human physiological as well as neurological diseases.https://www.frontiersin.org/articles/10.3389/fnins.2021.636454/fullmonosodium glutamateprotein aggregationnucleation-dependent polymerizationisothermal titration calorimetry measurementneurodegeneration |
| spellingShingle | Ishfaq Ahmad Ahanger Ishfaq Ahmad Ahanger Sania Bashir Zahoor Ahmad Parray Mohamed F. Alajmi Afzal Hussain Faizan Ahmad Md. Imtaiyaz Hassan Asimul Islam Anurag Sharma Rationalizing the Role of Monosodium Glutamate in the Protein Aggregation Through Biophysical Approaches: Potential Impact on Neurodegeneration Frontiers in Neuroscience monosodium glutamate protein aggregation nucleation-dependent polymerization isothermal titration calorimetry measurement neurodegeneration |
| title | Rationalizing the Role of Monosodium Glutamate in the Protein Aggregation Through Biophysical Approaches: Potential Impact on Neurodegeneration |
| title_full | Rationalizing the Role of Monosodium Glutamate in the Protein Aggregation Through Biophysical Approaches: Potential Impact on Neurodegeneration |
| title_fullStr | Rationalizing the Role of Monosodium Glutamate in the Protein Aggregation Through Biophysical Approaches: Potential Impact on Neurodegeneration |
| title_full_unstemmed | Rationalizing the Role of Monosodium Glutamate in the Protein Aggregation Through Biophysical Approaches: Potential Impact on Neurodegeneration |
| title_short | Rationalizing the Role of Monosodium Glutamate in the Protein Aggregation Through Biophysical Approaches: Potential Impact on Neurodegeneration |
| title_sort | rationalizing the role of monosodium glutamate in the protein aggregation through biophysical approaches potential impact on neurodegeneration |
| topic | monosodium glutamate protein aggregation nucleation-dependent polymerization isothermal titration calorimetry measurement neurodegeneration |
| url | https://www.frontiersin.org/articles/10.3389/fnins.2021.636454/full |
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