Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from Arabidopsis thaliana
1
Max-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476 Potsdam, Germany
2
Institute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria
*
Authors to whom correspondence should be addressed.
†
We dedicate this paper to the memory of our colleague Dirk K. Hincha who passed away during the preparation of this manuscript.
Academic Editor: Wim Van den Ende
Biomolecules 2021, 11(5), 615; https://doi.org/10.3390/biom11050615
Received: 31 March 2021
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Revised: 19 April 2021
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Accepted: 20 April 2021
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Published: 21 April 2021
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 (WTCg) 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.
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Keywords:
FTIR spectroscopy; sucrose; dehydration; LEA proteins; sugar glass; glass transition; hydrogen bonding
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MDPI and ACS Style
Hincha, D.K.; Zuther, E.; Popova, A.V. Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from Arabidopsis thaliana. Biomolecules 2021, 11, 615. https://doi.org/10.3390/biom11050615
AMA Style
Hincha DK, Zuther E, Popova AV. Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from Arabidopsis thaliana. Biomolecules. 2021; 11(5):615. https://doi.org/10.3390/biom11050615
Chicago/Turabian StyleHincha, Dirk K., Ellen Zuther, and Antoaneta V. Popova. 2021. "Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from Arabidopsis thaliana" Biomolecules 11, no. 5: 615. https://doi.org/10.3390/biom11050615
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