High critical temperature above T-g may contribute to the stability of biological systems

Citation
J. Buitink et al., High critical temperature above T-g may contribute to the stability of biological systems, BIOPHYS J, 79(2), 2000, pp. 1119-1128
Citations number
60
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOPHYSICAL JOURNAL
ISSN journal
00063495 → ACNP
Volume
79
Issue
2
Year of publication
2000
Pages
1119 - 1128
Database
ISI
SICI code
0006-3495(200008)79:2<1119:HCTATM>2.0.ZU;2-0
Abstract
In this study, we characterized the molecular mobility around T-g in sugars , poly-L-lysine and dry desiccation-tolerant biological systems, using ST-E PR,H-1-NMR, and FTIR spectroscopy, to understand the nature and composition of biological glasses. Two distinct changes in the temperature dependence of the rotational correlation time (tau(R)) of the spin probe 3-carboxy-pro xyl or the second moment (M-2) were measured in sugars and poly-L-lysine. W ith heating, the first change was associated with the melting of the glassy state (T-g). The second change (T-c), at which tau(R) abruptly decreased o ver several orders of magnitude, was found to correspond with the so-called cross-over temperature, where the dynamics changed from solid-like to liqu id-like. The temperature interval between T-g and T-c increased in the orde r of sucrose < trehalose < raffinose less than or equal to staychose < poly -L-lysine < biological tissues, from 17 to >50 degrees C, implying that the stability above T-g improved in the same order. These differences in tempe rature-dependent mobilities above T-g suggest that proteins rather than sug ars play an important role in the intracellular glass formation. The except ionally high T-c of intracellular glasses is expected to provide excellent long-term stability to dry organisms, maintaining a slow molecular motion i n the cytoplasm even at temperatures far above T-g.