Abstract
The biomolecules are known to be stabilized by osmolytes, trimethylamine-N-oxide (TMAO) while urea, destabilizes the protein structures. The deleterious effect of urea on proteins has been counteracted by TMAO is well understood; nonetheless, refolding of urea-induced conformational changes of proteins by TMAO is still an active subject. To understand the refolding ability of TMAO from urea-induced denaturation of biomolecules, we have performed transfer free energy (Δ G′ tr) and the hydrodynamic diameter ( d H ) of cyclic dipeptides (CDs) such as, cyclo(Gly–Gly), and cyclo(Leu–Ala) through solubilities and dynamic light scattering (DLS) measurements, respectively. We observed positive and negative values of Δ G′ tr for CDs from water to TMAO and urea, respectively. Our results reveal that TMAO is a refolding additive for urea deleterious actions on CDs at 1:1 and 1:2 molar ratios of TMAO and urea. However, TMAO (1 M) fails to refolding CDs structure from the urea (3–5 M)-induced conformational changes on CDs.
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