Abstract
Compatible osmolytes are a broad class of small organic molecules employed by living systems to combat environmental stress by enhancing the native protein structure. The molecular features that make for a superior biopreservation remain elusive. Through the use of time-resolved and steady-state spectroscopic techniques, in combination with molecular simulation, insight into what makes one molecule a more effective compatible osmolyte can be gained. Disaccharides differing only in their glycosidic bonds can exhibit different degrees of stabilization against thermal denaturation. The degree to which each sugar is preferentially excluded may explain these differences. The present work examines the biopreservation and hydration of trehalose, maltose, and gentiobiose.
Highlights
Osmolytes are a class of molecules used by living cells to maintain, regulate, and protect the formation of protein assemblies; they do so indirectly through the modification of the water structure and its activity within the cell [1,2,3,4]. Osmolytes such as disaccharide sugars are hypothesized to alter the structure of water near the surface of proteins, enhancing the stability of the protein structure, and reducing the tendency of the protein to denature under high-stress conditions
We extended our investigations of disaccharide sugars by comparing the hydration dynamics and thermal preservation properties of solutions containing trehalose, maltose, and gentiobiose, which have interesting differences in the hydration
Lysozyme can bind to the glycosidic bond and may interact with our disaccharide co-solutes
Summary
Osmolytes are a class of molecules used by living cells to maintain, regulate, and protect the formation of protein assemblies; they do so indirectly through the modification of the water structure and its activity within the cell [1,2,3,4]. Osmolytes such as disaccharide sugars are hypothesized to alter the structure of water near the surface of proteins, enhancing the stability of the protein structure, and reducing the tendency of the protein to denature under high-stress conditions (elevated temperature, pressure, high salinity, dehydration, and cryogenic temperatures). While it appears that for disaccharide molecules the thermal biopreservation capability of the molecules scaled with the water-structuring ability [14], the same was not found for smaller cyclic polyols [15]
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