In Situ Spectroscopic Quantification of Protein–Ice Interactions
2013
Twomey, Alan | Less, Rebekah | Kurata, Kosaku | Takamatsu, Hiroshi | Aksan, Alptekin
FTIR and confocal Raman microspectroscopy were used to measure interactions between albumin and ice in situ during quasi-equilibrium freezing in dimethyl sulfoxide (DMSO) solutions. At temperatures of −4 and −6 °C, albumin was found to be preferentially excluded from the ice phase during near-equilibrium freezing. This behavior reversed at lower temperatures. Instead, DMSO was preferentially excluded from the ice phase, resulting in an albumin concentration in the freeze-concentrated liquid phase that was lower than predicted. It is hypothesized that this was caused by the albumin in the freeze-concentrated liquid getting adsorbed onto the ice surface or becoming entrapped in the ice phase. It was observed that, under certain freezing protocols, as much as 20% of the albumin in solutions with starting concentrations of 32–53 mg/mL may be adsorbed onto the ice interface or entrapped in the ice phase.
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