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Inside Cover: Behavior of Lysozyme at the Electrified Water/Room Temperature Ionic Liquid Interface (Chem. Asian J. 11/2012)
Author(s) -
Alvarez de Eulate Eva,
Silvester Debbie S.,
Arrigan Damien W. M.
Publication year - 2012
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201290044
Subject(s) - ionic liquid , lysozyme , chemistry , adsorption , interface (matter) , ionic bonding , desorption , cover (algebra) , chromatography , analytical chemistry (journal) , nanotechnology , materials science , ion , organic chemistry , catalysis , biochemistry , mechanical engineering , gibbs isotherm , engineering
Protein behavior at the water–ionic liquid interface has been studied recently to better understand biological processes, biopharmaceutical stability, and bioanalytical measurements, and it can provide the foundations for new label‐free and sensitive biomolecular detection tools. In their Communication on page 2559 ff ., Damien W. M. Arrigan et al. studied lysozyme for the first time at the interface between water and the hydrophobic room‐temperature ionic liquid [FAP]. A preconcentration strategy based on constant‐potential adsorption followed by voltammetric desorption enables the detection of this protein.