Peptide interactions, phospholipid lipid membrane composition

Since the first attempt of Chapman and co-workers in 1966 [860], IR spectroscopy has become one of the most frequently used tools for elucidating lipid properties and the mutual effects of different lipids and proteins, which are of interest for different aspects of bioscience and biosensor design (see Refs. [333, 748, 861-864] for review). The IR methods used are transmission, ATR (MIR), and IRRAS for model monolayer, bilayer, and multibilayer membranes and biological membranes. To perform in situ measurements on the membranes of intact individual cells (e.g., as a function of cell membrane potential), planar miniature waveguides can be used instead of the ATR optics [865]. PM-IRRAS has been applied to obtain high-performance spectra of model membranes at the AW interface [866-875]. The experimental data focus mainly on the correlation between the structure of the matrix amphiphile or phospholipid film and the structure of the constituent species, the subphase composition, the surface pressure, and other external conditions, as well as the interaction of such monolayers with peptides and proteins (for reviews, see Refs. [332-334, 876, 877]). 

In the previous discussion it was suggested that membrane integration of intrinsic proteins could be facilitated by the interaction of hydrophobic regions of the nascent peptides with the phospholipids of the bilayer. Although it is assumed that the basic structure of the bilayer is the same for all membranes, the lipid compositions of various membranes show significant differences, both with respect to the relative proportions of the various phospholipids and their fatty substituents. In addition, some membranes may contain special types of lipids (sterols, sulfolipids, cardiolipin, etc.) that are absent in other membranes. It is also conceivable that there may exist regional differences in lipid composition within a single membrane. 

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