Water dynamics and stability of major blood proteins at pre-denaturation stage
We investigate the temperature effect on the size and stability of two major blood plasma proteins, human serum albumin and fibrinogen in aqueous NaCl solution. Dynamic Light Scattering measurements were carried out in the physiological temperature range up to 45°C. The analysis of the results provi...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Accademia Peloritana dei Pericolanti
2019-12-01
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| Series: | Atti della Accademia Peloritana dei Pericolanti : Classe di Scienze Fisiche, Matematiche e Naturali |
| Online Access: |
http://dx.doi.org/10.1478/AAPP.97S2A16
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| _version_ | 1818132400134160384 |
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| author | Natalia Atamas Vitalii Y. Bardik Serhiy Komisarenko Yevgen M. Makogonenko Edward V. Lugovskoi Nikolai P. Malomuzh Dmitry A. Nerukh Pavlo K. Solonin |
| author_facet | Natalia Atamas Vitalii Y. Bardik Serhiy Komisarenko Yevgen M. Makogonenko Edward V. Lugovskoi Nikolai P. Malomuzh Dmitry A. Nerukh Pavlo K. Solonin |
| author_sort | Natalia Atamas |
| collection | DOAJ |
| description | We investigate the temperature effect on the size and stability of two major blood plasma proteins, human serum albumin and fibrinogen in aqueous NaCl solution. Dynamic Light Scattering measurements were carried out in the physiological temperature range up to 45°C. The analysis of the results provided the temperature dependences of the macromolecular hydrodynamic radius and the ζ-potential. For albumin the hydrodynamic radius remained unchanged, while the ζ-potential increased sharply at approximately 40°C. For fibrinogen the radius increased significantly above 45°C and the ζ-potential increased similar to albumin at slightly below 40°C. The dynamics of albumin macromolecule was simulated using classical Molecular Dynamics, which showed no change in the gyration radius, root mean square deviation, and the composition of disulfide and salt bridges, but substantial change in the secondary structure of the protein. We conclude that these changes in the structure and dynamics of the proteins are correlated with the qualitative change of water dynamics at 42°C in the hydration shell of the proteins. |
| first_indexed | 2024-12-11T08:36:13Z |
| format | Article |
| id | doaj.art-399d309086fb44199476248e5bae5e5d |
| institution | Directory Open Access Journal |
| issn | 0365-0359 1825-1242 |
| language | English |
| last_indexed | 2024-12-11T08:36:13Z |
| publishDate | 2019-12-01 |
| publisher | Accademia Peloritana dei Pericolanti |
| record_format | Article |
| series | Atti della Accademia Peloritana dei Pericolanti : Classe di Scienze Fisiche, Matematiche e Naturali |
| spelling | doaj.art-399d309086fb44199476248e5bae5e5d2022-12-22T01:14:20ZengAccademia Peloritana dei PericolantiAtti della Accademia Peloritana dei Pericolanti : Classe di Scienze Fisiche, Matematiche e Naturali0365-03591825-12422019-12-0197S2A1610.1478/AAPP.97S2A16AAPP.97S2A16Water dynamics and stability of major blood proteins at pre-denaturation stageNatalia AtamasVitalii Y. BardikSerhiy KomisarenkoYevgen M. MakogonenkoEdward V. LugovskoiNikolai P. MalomuzhDmitry A. NerukhPavlo K. SoloninWe investigate the temperature effect on the size and stability of two major blood plasma proteins, human serum albumin and fibrinogen in aqueous NaCl solution. Dynamic Light Scattering measurements were carried out in the physiological temperature range up to 45°C. The analysis of the results provided the temperature dependences of the macromolecular hydrodynamic radius and the ζ-potential. For albumin the hydrodynamic radius remained unchanged, while the ζ-potential increased sharply at approximately 40°C. For fibrinogen the radius increased significantly above 45°C and the ζ-potential increased similar to albumin at slightly below 40°C. The dynamics of albumin macromolecule was simulated using classical Molecular Dynamics, which showed no change in the gyration radius, root mean square deviation, and the composition of disulfide and salt bridges, but substantial change in the secondary structure of the protein. We conclude that these changes in the structure and dynamics of the proteins are correlated with the qualitative change of water dynamics at 42°C in the hydration shell of the proteins. http://dx.doi.org/10.1478/AAPP.97S2A16 |
| spellingShingle | Natalia Atamas Vitalii Y. Bardik Serhiy Komisarenko Yevgen M. Makogonenko Edward V. Lugovskoi Nikolai P. Malomuzh Dmitry A. Nerukh Pavlo K. Solonin Water dynamics and stability of major blood proteins at pre-denaturation stage Atti della Accademia Peloritana dei Pericolanti : Classe di Scienze Fisiche, Matematiche e Naturali |
| title | Water dynamics and stability of major blood proteins at pre-denaturation stage |
| title_full | Water dynamics and stability of major blood proteins at pre-denaturation stage |
| title_fullStr | Water dynamics and stability of major blood proteins at pre-denaturation stage |
| title_full_unstemmed | Water dynamics and stability of major blood proteins at pre-denaturation stage |
| title_short | Water dynamics and stability of major blood proteins at pre-denaturation stage |
| title_sort | water dynamics and stability of major blood proteins at pre denaturation stage |
| url |
http://dx.doi.org/10.1478/AAPP.97S2A16
|
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