Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from <i>Arabidopsis thaliana</i>
Cells of many organisms and organs can withstand an (almost) total water loss (anhydrobiosis). Sugars play an essential role in desiccation tolerance due to their glass formation ability during dehydration. In addition, intrinsically disordered LEA proteins contribute to cellular survival under such...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-04-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/11/5/615 |
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| author | Dirk K. Hincha Ellen Zuther Antoaneta V. Popova |
| author_facet | Dirk K. Hincha Ellen Zuther Antoaneta V. Popova |
| author_sort | Dirk K. Hincha |
| collection | DOAJ |
| description | Cells of many organisms and organs can withstand an (almost) total water loss (anhydrobiosis). Sugars play an essential role in desiccation tolerance due to their glass formation ability during dehydration. In addition, intrinsically disordered LEA proteins contribute to cellular survival under such conditions. One possible mechanism of LEA protein function is the stabilization of sugar glasses. However, little is known about the underlying mechanisms. Here we used FTIR spectroscopy to investigate sucrose (Suc) glass stability dried from water or from two buffer components in the presence of four recombinant LEA and globular reference proteins. Buffer ions influenced the strength of the Suc glass in the order Suc < Suc/Tris < Suc/NaP. LEA proteins strengthened the sugar H-bonded network and the molecular structure in the glassy state. The position of νOH peak and the wavenumber–temperature coefficient (WTC<sub>g</sub>) provided similar information about the H-bonded network. Protein aggregation of LEA proteins was reduced in the desiccation-induced Suc glassy state. Detailed knowledge about the role of LEA proteins in the stabilization of dry sugar glasses yields information about their role in anhydrobiosis. This may open the possibility to use such proteins in biotechnical applications requiring dry storage of biologicals such as proteins, cells or tissues. |
| first_indexed | 2024-03-10T12:07:46Z |
| format | Article |
| id | doaj.art-9397c86427004825869fd756c2eadd99 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T12:07:46Z |
| publishDate | 2021-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-9397c86427004825869fd756c2eadd992023-11-21T16:27:47ZengMDPI AGBiomolecules2218-273X2021-04-0111561510.3390/biom11050615Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from <i>Arabidopsis thaliana</i>Dirk K. Hincha0Ellen Zuther1Antoaneta V. Popova2Max-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476 Potsdam, GermanyMax-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476 Potsdam, GermanyMax-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476 Potsdam, GermanyCells of many organisms and organs can withstand an (almost) total water loss (anhydrobiosis). Sugars play an essential role in desiccation tolerance due to their glass formation ability during dehydration. In addition, intrinsically disordered LEA proteins contribute to cellular survival under such conditions. One possible mechanism of LEA protein function is the stabilization of sugar glasses. However, little is known about the underlying mechanisms. Here we used FTIR spectroscopy to investigate sucrose (Suc) glass stability dried from water or from two buffer components in the presence of four recombinant LEA and globular reference proteins. Buffer ions influenced the strength of the Suc glass in the order Suc < Suc/Tris < Suc/NaP. LEA proteins strengthened the sugar H-bonded network and the molecular structure in the glassy state. The position of νOH peak and the wavenumber–temperature coefficient (WTC<sub>g</sub>) provided similar information about the H-bonded network. Protein aggregation of LEA proteins was reduced in the desiccation-induced Suc glassy state. Detailed knowledge about the role of LEA proteins in the stabilization of dry sugar glasses yields information about their role in anhydrobiosis. This may open the possibility to use such proteins in biotechnical applications requiring dry storage of biologicals such as proteins, cells or tissues.https://www.mdpi.com/2218-273X/11/5/615FTIR spectroscopysucrosedehydrationLEA proteinssugar glassglass transition |
| spellingShingle | Dirk K. Hincha Ellen Zuther Antoaneta V. Popova Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from <i>Arabidopsis thaliana</i> Biomolecules FTIR spectroscopy sucrose dehydration LEA proteins sugar glass glass transition |
| title | Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from <i>Arabidopsis thaliana</i> |
| title_full | Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from <i>Arabidopsis thaliana</i> |
| title_fullStr | Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from <i>Arabidopsis thaliana</i> |
| title_full_unstemmed | Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from <i>Arabidopsis thaliana</i> |
| title_short | Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from <i>Arabidopsis thaliana</i> |
| title_sort | stabilization of dry sucrose glasses by four lea 4 proteins from i arabidopsis thaliana i |
| topic | FTIR spectroscopy sucrose dehydration LEA proteins sugar glass glass transition |
| url | https://www.mdpi.com/2218-273X/11/5/615 |
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