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• W4225283346 abstract "The amphiphilicity and denaturation efficiency of urea can be tuned via alkylation. Although the interaction of alkylureas with water and proteins has been studied in detail, hydration of 1-methylurea has remained elusive, precluding the isolation of the effect of an individual methyl group. Here, we study water dynamics in the hydration shell of 1-methylurea (1-MU) using infrared absorption and ultrafast infrared spectroscopies. We find that 1-MU hardly affects the hydrogen-bond distribution of water as probed by the OD stretching vibration of HOD molecules. Polarization resolved infrared pump-probe experiments reveal that 1-MU slows down the rotational dynamics of up to 3 water molecules in its hydration shell. A comparison to earlier results for other alkylureas suggests that further alkylation does not necessarily slow down the rotational dynamics of additional water molecules. Two-dimensional infrared experiments show that 1-MU markedly slows down the hydrogen-bond fluctuation dynamics of water, yet similar to what has been found for urea and dimethylureas. Remarkably, (alkyl-)ureas that share a similar effect on water's hydrogen-bond fluctuation dynamics have a similar (modest) protein denaturation tendency. As such, not only the hydrophobicity but also hydration of hydrophilic fragments of alkylureas may be relevant to explain their function toward biomolecules." @default.
• W4225283346 created "2022-05-05" @default.
• W4225283346 creator A5013053675 @default.
• W4225283346 creator A5084395025 @default.
• W4225283346 date "2022-04-27" @default.
• W4225283346 modified "2023-09-30" @default.
• W4225283346 title "A single methyl group drastically changes urea’s hydration dynamics" @default.
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• W4225283346 doi "https://doi.org/10.1063/5.0085461" @default.
• W4225283346 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35490020" @default.
• W4225283346 hasPublicationYear "2022" @default.
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