Conformational Consequences for Compatible Osmolytes on Thermal Denaturation

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.

Automated summary

This study investigates the biopreservation and hydration effects of trehalose, maltose, and gentiobiose on proteins. It is found that despite differences only in their glycosidic bonds, these disaccharides exhibit varying degrees of stabilization against thermal denaturation due to differences in their preferential exclusion.