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Abstract
Tethered bilayer lipid membranes (tBLMs) consist of a lipid bilayer interposed between an aqueous solution and a hydrophilic “spacer” anchored to a gold or mercury electrode. There is great potential for application of these biomimetic membranes for the elucidation of structure-function relationships of membrane peptides and proteins. A drawback in the use of mercury-supported tBLMs with respect to gold-supported ones is represented by the difficulty in applying surface sensitive, spectroscopic and scanning probe microscopic techniques to gather information on the architecture of these biomimetic membranes. Nonetheless, mercury-supported tBLMs are definitely superior to gold-supported biomimetic membranes for the investigation of the function of membrane peptides and proteins, thanks to a fluidity and lipid lateral mobility comparable with those of bilayer lipid membranes interposed between two aqueous phases (BLMs), but with a much higher robustness and resistance to electric fields. The different features of mercury-supported tBLMs reconstituted with functionally active membrane proteins and peptides of bacteriological or pharmacological interest may be disclosed by a judicious choice of the most appropriate electrochemical techniques. We will describe the way in which electrochemical impedance spectroscopy, potential-step chronocoulometry, cyclic voltammetry and phase-sensitive AC voltammetry are conveniently employed to investigate the structure of mercury-supported tBLMs and the mode of interaction of antimicrobial peptides reconstituted into them.
Highlights
In view of the complexity and diversity of the functions performed by the different peptides and proteins embedded in a biomembrane it has been found expedient to incorporate them singly into experimental models of cell membranes, so as to isolate and investigate their functions
Several efforts are presently made to realize biomimetic membranes consisting of a lipid bilayer anchored to a metal electrode through a hydrophilic spacer and satisfying those requirements of ruggedness, fluidity and high electrical resistance that are necessary for the incorporation of integral proteins in a functionally active state
Mercury is a advantageous support for Tethered bilayer lipid membranes (tBLMs), since it imparts to the lipid bilayer a fluidity and lipid lateral mobility not shared by solid supports such as gold and silver
Summary
In view of the complexity and diversity of the functions performed by the different peptides and proteins embedded in a biomembrane it has been found expedient to incorporate them singly into experimental models of cell membranes, so as to isolate and investigate their functions. Tethered bilayer lipid membranes (tBLMs) are versatile model systems that provide a defined platform for the incorporation of peptides and proteins and for the investigation of their functional activity [1,2,3] They are obtained by tethering a “thiolipid” monolayer to the surface of a noble metal such as Au, Ag or Hg. Thiolipid molecules consist of a hydrophilic chain (the spacer) terminated at one end with a sulfhydryl or disulfide group for anchoring to the support and covalently linked at the other end to two alkyl chains simulating the hydrocarbon tails of a lipid. The defect-free support provided by liquid mercury to the lipid monolayer and the complete absence of solvent in the film impart high fluidity, lipid lateral mobility, mechanical stability, resistance to electric fields and reproducibility to the monolayer This self-assembly procedure exploits the fact that mercury is the most hydrophobic metal. In this contribution we will describe the way in which these different techniques are conveniently employed to investigate the structure of mercury-supported tBLMs and the mode of interaction of antimicrobial peptides reconstituted into them
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