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Trehalose published paper abstract - Organization and mobility of water in amorphous and crystalline E-mail

Nature Materials 5, 632 - 635 (2006)
doi:10.1038/nmat1681

Organization and mobility of water in amorphous and crystalline trehalose

Duncan Kilburn, Sam Townrow, Vincent Meunier, Robert Richardson, Ashraf Alam and Job Ubbink

The disaccharide trehalose is accumulated by microorganisms, such as yeasts, and multicellular organisms, such as tardigrades, when conditions of extreme drought occur. In this way these organisms can withstand dehydration through the formation of an intracellular carbohydrate glass, which, with its high viscosity and hydrogen-bonding interactions, stabilizes and protects the integrity of complex biological structures and molecules. This property of trehalose can also be harnessed in the stabilization of liposomes, proteins and in the preservation of red blood cells, but the underlying mechanism of bioprotection is not yet fully understood. Here we use positron annihilation lifetime spectroscopy to probe the free volume of trehalose matrices; specifically, we develop a molecular picture of the organization and mobility of water in both amorphous and crystalline states. Whereas in amorphous matrices, water increases the average intermolecular hole size, in the crystalline dihydrate it is organized as a confined one-dimensional fluid in channels of fixed diameter that allow activated diffusion of water in and out of the crystallites. We present direct real-time evidence of water molecules unloading reversibly from these channels, thereby acting as both a sink and a source of water in low-moisture systems. We postulate that this behaviour may provide the overall stability required to keep organisms viable through dehydration conditions.

 

1.       H.H. Wills Physics Laboratory, University of Bristol, Tyndall Avenue, Bristol BS8 1TL, UK

2.       Nestlé Research Center, Vers-chez-les-Blanc, CH-1000 Lausanne 26, Switzerland


Source
Trehalose Can Extend Shelf Life of Other Sugars E-mail

J Zhejiang Univ Sci B. 2006 February; 7(2): 85–89.
Published online 2006 January 19. doi: 10.1631/jzus.2006.B0085.

 
Copyright © 2006, Journal of Zhejiang University Science

 

Crystallization inhibition of an amorphous sucrose system using raffinose*
K.M. Leinen and T.P. Labuza†
Department of Food Science and Nutrition, University of Minnesota, St. Paul, MN 55108, USA
†E-mail:tplabuza@umn.edu

Abstract

The shelf life of pure amorphous sucrose systems, such as cotton candy, can be very short. Previous studies have shown that amorphous sucrose systems held above the glass transition temperature will collapse and crystallize. One study, however, showed that adding a small percent of another type of sugar, such as trehalose, to sucrose can extend the shelf life of the amorphous system by slowing crystallization. This study explores the hypothesis that raffinose increases the stability of an amorphous sucrose system. Cotton candy at 5 wt% raffinose and 95 wt% sucrose was made and stored at room temperature and three different relative humidities (%RH) 11%RH, 33%RH, and 43%RH. XRD patterns, and glass transition temperatures were obtained to determine the stability as a function of %RH. The data collected showed that raffinose slows sucrose crystallization in a low moisture amorphous state above the glass transition temperature and therefore improves the stability of amorphous sucrose systems.

Source
Trehalose Improves Stress Tolerance in Organisms E-mail

A bifunctional TPS-TPP enzyme from yeast confers tolerance to multiple and extreme abiotic-stress conditions in transgenic Arabidopsis

Miranda, José * ; Avonce, Nelson; Suárez, Ramón; Thevelein, Johan; Van Dijck, Patrick; Iturriaga, Gabriel

Improving stress tolerance is a major goal for agriculture. Trehalose is a key molecule involved in drought tolerance in anhydrobiotic organisms. Here we describe the construction of a chimeric translational fusion of yeast trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase. This construct was overexpressed in yeast cells displaying both TPS and TPP enzyme activities and trehalose biosynthesis capacity. In Arabidopsis thaliana, the gene fusion was overexpressed using either the 35S promoter or the stress-regulated rd29A promoter. Transgene insertion in the genome was checked by PCR and transcript expression by RT-PCR. Several independent homozygous lines were selected in the presence of kanamycin and further analyzed.

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Trehalose Used in Cryopreservation of Human Fetal Skin for Transplantation E-mail

Cryopreservation of fetal skin is improved by extracellular trehalose

Gulsun Erdag, Ali Eroglu, Jeffrey R. Morgan and Mehmet Toner
Center for Engineering in Medicine and Surgical Services, Massachusetts General Hospital and Harvard Medical School, Shriners Burns Hospital, Boston, MA 02114, USA

Abstract

In this study, we tested a non-permeating cryoprotectant, trehalose, in combination with dimethyl sulfoxide (Me2SO) in the cryopreservation of human fetal skin and compared it to Me2SO and glycerol, protocols that are routinely used by skin banks. The viability of fetal skin from four groups (fresh, and cryopreserved with glycerol, Me2SO, or trehalose/Me2SO) were evaluated using an in vitro membrane integrity assay and by transplantation to immunodeficient mice. The membrane integrity assay showed a 90% integrity in fresh, unfrozen fetal skin.

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Trehalose Proves Effective Kinetic Advantages E-mail

Characterization of a Bifunctional Enzyme Fusion of Trehalose-6-Phosphate Synthetase and Trehalose-6-Phosphate Phosphatase of Escherichia coli

Hak Soo Seo,1 Yeon Jong Koo,1 Jae Yun Lim,1 Jong Tae Song,1 Chung Ho Kim,2 Ju Kon Kim,3 Jong Seob Lee,4 and Yang Do Choi1

Graduate School of Agricultural Biotechnology, Seoul National University, Suwon 441-744,1 Department of Food and Nutrition, Seowon University, Cheongju 361-742,2 Department of Biological Science, MyongJi University, Yongin 449-728,3 and Graduate School of Biological Sciences, Seoul National University, Seoul 151-742,4 Korea

ABSTRACT

To test the effect of the physical proximity of two enzymes catalyzing sequential reactions, a bifunctional fusion enzyme, TPSP, was constructed by fusing the Escherichia coli genes for trehalose-6-phosphate (T6P) synthetase (TPS) and trehalose-6-phosphate phosphatase (TPP). TPSP catalyzes the sequential reaction in which T6P is formed and then dephosphorylated, leading to the synthesis of trehalose.

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Trehalose Poster at International Conference on Molecular Systems Biology E-mail

Poster Title: 13C-NMR to monitor online the kinetics of intracellular metabolite pools in response to heat stress: input data for modeling the trehalose cycle in Saccharomyces cerevisiae

10th International Conference on Molecular Systems Biology
February 25-28, 2008, University of the Philippines, Diliman, Quezon City

Authors: L. Fonseca, C. Sanchez, J. Wu, H. Santos, and E.O. Voit
Presentor: Luis Fonseca (Universidade Nova de Lisboa, Portugal)

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Trehalose puts life on hold E-mail

Authored by John Bonner, and published in Chemistry World, 28 July 2005
Reproduced by permission from the Royal Society of Chemistry.

Researchers are discovering how an apparently ordinary disaccharide helps plants and animals survive extraordinary environments.

Salvatore Magazù and colleagues at the University of Messina, Italy, have used a specialized spectroscopic technique to examine interactions between molecules of trehalose and water.

“The results could explain the unique biological properties of trehalose,” said the researchers, “which are not shared by other sugars with identical chemical formulae.”

Trehalose (C12H22O11) is a common component in the cells of many plant and animal roups. It protects desert species from damage during periods of drought and can promote survival in extreme heat and cold.

Several theories have been proposed as to why trehalose exerts far greater protective effects than other disaccharides like sucrose and maltose. These include suggestions that its special properties are due to a higher glass transition temperature or that it forms direct hydrogen bonds with lipids in cells, replacing similar bonds with water molecules.
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Trehalose alleviates polyglutamine-mediated pathology in mouse model of Huntington disease E-mail

Nat Med. 2004 Feb;10(2):123-4.

Tanaka M, Machida Y, Niu S, Ikeda T, Jana NR, Doi H, Kurosawa M, Nekooki M,
Nukina N. Laboratory for Structural Neuropathology, RIKEN Brain Science
Institute, 2-1 Hirosawa, Wako City, Saitama 351-0198, Japan.

Abstract:

Inhibition of polyglutamine-induced protein aggregation could provide treatment
options for polyglutamine diseases such as Huntington disease. Here we showed
through in vitro screening studies that various disaccharides can inhibit
polyglutamine-mediated protein aggregation. We also found that various
disaccharides reduced polyglutamine aggregates and increased survival in a cellular
model of Huntington disease. Oral administration of trehalose, the most effective of
these disaccharides, decreased polyglutamine aggregates in cerebrum and liver,
improved motor dysfunction and extended lifespan in a transgenic mouse model of
Huntington disease. We suggest that these beneficial effects are the result of
trehalose binding to expanded polyglutamines and stabilizing the partially unfolded
polyglutamine-containing protein. Lack of toxicity and high solubility, coupled with
efficacy upon oral administration, make trehalose promising as a therapeutic drug
or lead compound for the treatment of polyglutamine diseases. The saccharidepolyglutamine
interaction identified here thus provides a new therapeutic strategy for
polyglutamine diseases.
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