FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts
The effect of neutral salts on protein conformation was first analyzed by Hofmeister in 1888, however, even today this phenomenon is not completely understood. To clarify this effect, we studied changes in the secondary structure of two proteins: human serum albumin with predominantly α-helical stru...
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MDPI AG
2020-04-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/10/4/606 |
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| author | Dmitrii Usoltsev Vera Sitnikova Andrey Kajava Mayya Uspenskaya |
| author_facet | Dmitrii Usoltsev Vera Sitnikova Andrey Kajava Mayya Uspenskaya |
| author_sort | Dmitrii Usoltsev |
| collection | DOAJ |
| description | The effect of neutral salts on protein conformation was first analyzed by Hofmeister in 1888, however, even today this phenomenon is not completely understood. To clarify this effect, we studied changes in the secondary structure of two proteins: human serum albumin with predominantly α-helical structure and porcine pancreas β-trypsin with the typical β-structural arrangement in aqueous solutions of neutral salts (KSCN, KCl, (NH<sub>4</sub>)<sub>2</sub>SO<sub>4</sub>). The changes in the secondary structure were studied at 23 °C and 80 °C by using the second derivative deconvolution method of the IR spectra. Our results demonstrated that the ability of the salts to stabilize/destabilize these two proteins correlates with the Hofmeister series of ions. At the same time, some exceptions were also observed. The destabilization of the native structures of both α-helical albumin and β-structural trypsin upon interaction with neutral salts leads to the formation of intermolecular β-sheets typical for amyloid fibrils or amorphous aggregates. Thus, our quantitative FTIR-spectroscopy analysis allowed us to further clarify the mechanisms and complexity of the neutral salt actions on protein structures which may lead to strategies preventing unwelcome misfolding of proteins. |
| first_indexed | 2024-03-10T20:29:08Z |
| format | Article |
| id | doaj.art-87831b01f712422f996494be2db64986 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T20:29:08Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
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| series | Biomolecules |
| spelling | doaj.art-87831b01f712422f996494be2db649862023-11-19T21:34:04ZengMDPI AGBiomolecules2218-273X2020-04-0110460610.3390/biom10040606FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral SaltsDmitrii Usoltsev0Vera Sitnikova1Andrey Kajava2Mayya Uspenskaya3Department of Applied Optics, ITMO University, St.-Petersburg 197101, RussiaDepartment of Applied Optics, ITMO University, St.-Petersburg 197101, RussiaInternational Research Institute of Bioengineering, ITMO University, St.-Petersburg 197101, RussiaDepartment of Applied Optics, ITMO University, St.-Petersburg 197101, RussiaThe effect of neutral salts on protein conformation was first analyzed by Hofmeister in 1888, however, even today this phenomenon is not completely understood. To clarify this effect, we studied changes in the secondary structure of two proteins: human serum albumin with predominantly α-helical structure and porcine pancreas β-trypsin with the typical β-structural arrangement in aqueous solutions of neutral salts (KSCN, KCl, (NH<sub>4</sub>)<sub>2</sub>SO<sub>4</sub>). The changes in the secondary structure were studied at 23 °C and 80 °C by using the second derivative deconvolution method of the IR spectra. Our results demonstrated that the ability of the salts to stabilize/destabilize these two proteins correlates with the Hofmeister series of ions. At the same time, some exceptions were also observed. The destabilization of the native structures of both α-helical albumin and β-structural trypsin upon interaction with neutral salts leads to the formation of intermolecular β-sheets typical for amyloid fibrils or amorphous aggregates. Thus, our quantitative FTIR-spectroscopy analysis allowed us to further clarify the mechanisms and complexity of the neutral salt actions on protein structures which may lead to strategies preventing unwelcome misfolding of proteins.https://www.mdpi.com/2218-273X/10/4/606protein denaturationFTIR spectroscopysecond derivative methodsecondary structureneutral saltsaggregates |
| spellingShingle | Dmitrii Usoltsev Vera Sitnikova Andrey Kajava Mayya Uspenskaya FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts Biomolecules protein denaturation FTIR spectroscopy second derivative method secondary structure neutral salts aggregates |
| title | FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts |
| title_full | FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts |
| title_fullStr | FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts |
| title_full_unstemmed | FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts |
| title_short | FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts |
| title_sort | ftir spectroscopy study of the secondary structure changes in human serum albumin and trypsin under neutral salts |
| topic | protein denaturation FTIR spectroscopy second derivative method secondary structure neutral salts aggregates |
| url | https://www.mdpi.com/2218-273X/10/4/606 |
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