In Situ Spectroscopic Quantification of Protein-Ice Interactions

Alan Twomey, Rebekah Less, Kosaku Kurata, Hiroshi Takamatsu, Alptekin Aksan

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)7889-7897
Number of pages9
JournalJournal of Physical Chemistry B
Volume117
Issue number26
DOIs
StatePublished - Jul 3 2013

Fingerprint Dive into the research topics of 'In Situ Spectroscopic Quantification of Protein-Ice Interactions'. Together they form a unique fingerprint.

Cite this