Abstract
Dimethyl sulfoxide (DMSO) increases cell and tissue viability at low temperatures and is commonly used as a cryoprotectant for cryogenic storage of biological materials. DMSO disorders the water hydrogen-bond networks and inhibits ice-crystal growth, though the specific DMSO interactions with water are difficult to characterize. In this study, we use a combination of Fourier Transform infrared spectroscopy (FTIR), molecular dynamics simulations, and vibrational frequency maps to characterize the temperature-dependent hydrogen bonding interactions of DMSO with water from 30 °C to −80 °C. Specifically, broad peaks in O–D stretch vibrational spectra of DMSO and deuterated water (HDO) cosolvent systems show that the hydrogen bond networks become increasingly disrupted compared to pure water. Simulations demonstrated that these disrupted hydrogen bond networks remain largely localized to the first hydration shell of DMSO, which explains the high DMSO concentrations needed to prevent ice crystal formation in cryopreservation applications.
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