PMID- 27159556
OWN - NLM
STAT- MEDLINE
DCOM- 20170913
LR  - 20171213
IS  - 1526-4602 (Electronic)
IS  - 1525-7797 (Linking)
VI  - 17
IP  - 6
DP  - 2016 Jun 13
TI  - Lysozyme Solubility and Conformation in Neat Ionic Liquids and Their Mixtures 
      with Water.
PG  - 2233-9
LID - 10.1021/acs.biomac.6b00468 [doi]
AB  - The room temperature solubility of a number of model proteins is assessed for a 
      diverse set of neat ionic liquids (ILs). For two soluble protein-IL pairs, 
      lysozyme in [C2MIM][EtSO4] (1-ethyl-3-methylimidazolium ethylsulfate) and in 
      [C2,4,4,4P][Et2PO4] (tributyl(ethyl)phosphonium diethylphosphate), protein 
      solubility and structure at various temperatures are probed by dynamic light 
      scattering (assessing dissolved molecular size), turbidimetry (reflecting degree 
      of solubility), and Fourier transform infrared spectroscopy (uncovering helical 
      secondary structure). As compared to aqueous environments, [C2,4,4,4P][Et2PO4] 
      thermally stabilizes protein size and secondary structure while [C2MIM][EtSO4] 
      does the opposite. Lysozyme denatured in [C2MIM][EtSO4] does not aggregate, 
      presumably due to an absence of hydrophobic interactions, and the denaturation 
      appears thermally reversible. Both ILs at room temperature are miscible with 
      water in all proportions, but to create the corresponding ternary mixtures with 
      protein, the order of mixing is important. Mixed to avoid additions of water to 
      IL-dissolved protein, stable solutions are obtained with [C2MIM][EtSO4] at all 
      solvent compositions. When water is added to IL-rich solutions, liquid-liquid 
      demixing is noted.
FAU - Strassburg, Stephen
AU  - Strassburg S
AD  - Polymer Science and Engineering Department, University of Massachusetts-Amherst , 
      Amherst, Massachusetts 01003, United States.
FAU - Bermudez, Harry
AU  - Bermudez H
AD  - Polymer Science and Engineering Department, University of Massachusetts-Amherst , 
      Amherst, Massachusetts 01003, United States.
FAU - Hoagland, David
AU  - Hoagland D
AD  - Polymer Science and Engineering Department, University of Massachusetts-Amherst , 
      Amherst, Massachusetts 01003, United States.
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20160520
PL  - United States
TA  - Biomacromolecules
JT  - Biomacromolecules
JID - 100892849
RN  - 0 (Ionic Liquids)
RN  - 059QF0KO0R (Water)
RN  - EC 3.2.1.- (hen egg lysozyme)
RN  - EC 3.2.1.17 (Muramidase)
SB  - IM
MH  - Animals
MH  - Chickens
MH  - Ionic Liquids/*chemistry
MH  - Muramidase/*chemistry/metabolism
MH  - Protein Structure, Secondary
MH  - Solubility
MH  - Spectroscopy, Fourier Transform Infrared
MH  - Temperature
MH  - Water/*chemistry
EDAT- 2016/05/10 06:00
MHDA- 2017/09/14 06:00
CRDT- 2016/05/10 06:00
PHST- 2016/05/10 06:00 [entrez]
PHST- 2016/05/10 06:00 [pubmed]
PHST- 2017/09/14 06:00 [medline]
AID - 10.1021/acs.biomac.6b00468 [doi]
PST - ppublish
SO  - Biomacromolecules. 2016 Jun 13;17(6):2233-9. doi: 10.1021/acs.biomac.6b00468. 
      Epub 2016 May 20.