Membrane mimetic systems
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Fluorescence imaging and vibrational spectroscopy methods (namely Infrared and Raman spectroscopy) have been applied widely herein for studying membrane mimetic systems, with widespread applications. The effect of surfactant protein B on phospholipid films have been analyzed both at the air-water interface and as thin films on metal substrates that provided important morphological and structural information involving the lipid dynamics and the secondary structures of the protein (Chapters 3, 4). Raman spectroscopy also provided an insight on the conformations of the disulfide bonds, which are of prime importance in protein folding (Chapter 5). In addition, biotin functionalized phospholipid bolaamphiphiles have been successfully used for fabricating supported membranes that demonstrated extended stability in vitro (Chapter 6). The design of these bolaamphiphiles was based on the ‘tail-to-tail’ coupling of the archae lipids. Polarization modulation infrared reflection absorption spectroscopy of the Langmuir-Blodgett deposited films of these lipids on polyelectrolyte coated metal substrates, revealed the effect of spacer groups utilized for biotin functionalization. Chapter 7 describes the study of an amphiphilic protein block copolymer (B9) that exhibited stimuli responsive conformational flexibility, in solution. Of note was the thermally induced micelle size change that was found to be triggered by the conformational changes in the protein secondary structures. Such a system could potentially function as a ‘protein switch’, where the response to the external stimulus could also be manipulated by sequence alterations.