title: Dynamics of loop 1 of domain I in human serum albumin when dissolved in ionic liquids.
abstract: We report on the rotational reorientation dynamics associated with loop 1 of domain I within a large multidomain protein (human serum albumin, HSA) when it is dissolved in binary mixtures of ionic liquid (1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide ([C4mim][Tf2N]), 1-butyl-3-methylimidazolium tetrafluoroborate ([C4mim][BF4]), or 1-butyl-3-methylimidazolium hexafluorophosphate ([C4mim][PF6])) and distilled deionized water (ddH2O) as a function of temperature and water loading. In IL/2% ddH2O (v/v) mixtures, loop 1 of domain I is more significantly denatured in comparison to the protein dissolved in aqueous solutions containing strong chemical denaturants (e.g., 8 M guanidine HCl (Gu.HCl) or urea). As water loading increases, there is evidence for progressive refolding of loop 1 of domain I followed by recoupling with domains I, II, and III in the [C4mim][BF4]/ddH2O mixtures at 20 degrees C. Above 30% (v/v) water, where domain I appears refolded, the Ac reporter molecule's semiangle steadily decreases from 35 degrees to 20 degrees with increasing water loading. From the perspective of domain I in HSA, this behavior is similar to the effects of dilution from 4 to 0 M Gu.HCl in aqueous solution. Overall, these results lend insight into the tangle of biocatalytic and structural/dynamical mechanisms that enzymes may undergo in ionic liquid-based systems. It will be particularly motivating to extend this work to include enzyme-attuned ionic liquids shown to improve biocatalytic performance beyond that possible in the native (predominantly aqueous) setting.
authors.affiliation: Department of Chemistry, Natural Sciences Complex, University at Buffalo, The State University of New York, Buffalo, New York 14260-3000, USA.
authors.forename: Taylor A
authors.initials: TA
authors.lastname: Page
authors.forename: Nadine D
authors.initials: ND
authors.lastname: Kraut
authors.forename: Phillip M
authors.initials: PM
authors.lastname: Page
authors.forename: Gary A
authors.initials: GA
authors.lastname: Baker
authors.forename: Frank V
authors.initials: FV
authors.lastname: Bright
mesh_terms: D006801:Humans; D052578:Ionic Liquids / Q000737:chemistry*; D008958:Models, Molecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000737:chemistry*; D013696:Temperature; D014867:Water / Q000737:chemistry
chemical_list: D052578:Ionic Liquids; D012709:Serum Albumin; D014867:Water