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Dynamic Mass Transfer of Hemoglobin at the Aqueous/Ionic-Liquid Interface Monitored with Liquid Core Optical
Xuwei Chen1, Xu Yang1, Wanying Zeng1
1Research Center for Analytical Sciences, Northeastern University, Heping District, Wenhua Road 3-11, Shenyang 110819, China.
Langmuir : the ACS Journal of Surfaces and Colloids
|July 15, 2015
Summary
This study monitored hemoglobin (Hb) transfer between aqueous and ionic liquid phases using an optical waveguide. Hemoglobin transfer is driven by interactions between its heme group and ionic liquid cations, with hydrophobic forces also contributing.
Area of Science:
- Biochemistry
- Materials Science
- Analytical Chemistry
Background:
- Protein isolation from biological samples is crucial.
- Ionic liquids offer unique properties for biomolecule manipulation.
- Monitoring dynamic protein transfer is challenging.
Purpose of the Study:
- To develop an optical waveguide system for real-time monitoring of hemoglobin (Hb) mass transfer.
- To investigate the dynamics of Hb transfer at the aqueous/ionic liquid interface.
- To elucidate the driving forces behind Hb transfer into ionic liquids.
Main Methods:
- Fabrication of a solid-cladding/liquid-core/liquid-cladding sandwich optical waveguide.
- Utilizing a hydrophobic ionic liquid (1,3-dibutylimidazolium hexafluorophosphate, BBimPF6) as the core.
- Monitoring Hb transfer using UV-vis spectroscopy via optical fibers and a CCD spectrophotometer.
Main Results:
- Observed Hb accumulation at the aqueous/ionic liquid interface followed by extraction into the ionic liquid.
- Demonstrated that a portion of Hb remains at the interface post-transfer.
- Identified coordination interactions between Hb's heme group and ionic liquid cations as the primary driver, with hydrophobic interactions also playing a role.
Conclusions:
- The developed optical waveguide system effectively monitors dynamic protein mass transfer.
- Hb transfer into ionic liquids is a complex process influenced by specific molecular interactions.
- Understanding these interactions is key for optimizing protein isolation and purification strategies.
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