Hydrophobic interactions of sucralose with protein structures

Sucralose is a commonly employed artificial sweetener that appears to destabilize protein native structures. This is in direct contrast to the bio-preservative nature of its natural counterpart, sucrose, which enhances the stability of biomolecules against environmental stress. We have further explo...

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Bibliographic Details
Published in:Archives of biochemistry and biophysics 2018-02, Vol.639, p.38-43
Main Authors: Shukla, Nimesh, Pomarico, Enrico, Hecht, Cody J.S., Taylor, Erika A., Chergui, Majed, Othon, Christina M.
Format: Article
Language:English
Subjects:
Disaccharide
Hydration dynamics
Hydrophobic-hydrophobic interaction
Kosmotrope
Osmolyte
Preferential exclusion
Protein stability
Solvation
Sucralose
Sucrose
Time-resolved fluorescence up-conversion spectroscopy
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Summary:Sucralose is a commonly employed artificial sweetener that appears to destabilize protein native structures. This is in direct contrast to the bio-preservative nature of its natural counterpart, sucrose, which enhances the stability of biomolecules against environmental stress. We have further explored the molecular interactions of sucralose as compared to sucrose to illuminate the origin of the differences in their bio-preservative efficacy. We show that the mode of interactions of sucralose and sucrose in bulk solution differ subtly through the use of hydration dynamics measurement and computational simulation. Sucralose does not appear to disturb the native state of proteins for moderate concentrations (
ISSN:0003-9861
1096-0384
DOI:10.1016/j.abb.2017.12.013