Lipid-protein interactions amphiphiles, role

Among the diverse components of biomembranes, lipids are essential in structural aspects. Lipids are defined operationally as derivatives of fatty acids and their metabolites. As lipids are usually amphiphilic molecules with hydrophobic hydrocarbon tails and hydrophilic head groups (as shown in Figure 1), the bilayer structures of biomembranes are held with hydrophobic forces to the tails and heads of lipids. Another major component of biomembranes is proteins. The weight proportion of proteins in biomembranes is often more than that of lipids. As proteins are more rigid than lipid assemblies, specific interactions by biomembranes are often related to proteins. Further, the sterols contained in biomembranes play unique roles in their apolar regions. As the functionality of biomembranes arises from the diversity of their composition, various kinds of molecules have been studied for biomembrane modeling. 

It is now well established that proteins can induce phase transitions in lipid membranes, resulting in new structures not found in pure lipid-water systems (c/. section 5.1). However, this property is not peculiar to proteins the same effect can be induced by virtually any amphiphilic molecule. Depending on the structure and nature of proteins, their interactions with lipid bilayers can be manifested in very different ways. We may further assume that the role of proteins in the biogenesis of cubic membranes is analogous to that in condensed systems, and lipids are necessary for the formation of a cubic membrane. This assumption is supported by studies of membrane oxidation, which induce a structure-less proteinaceous mass [113]. However, the existence of a lipid bilayer by itself does not guarantee the formation of a cubic membrane, as proteins may also play an essential role in setting the membrane curvature. In this context, note that the presence of chiral components e.g. proteins) may induce saddle-shaped structures characteristic of cubic membranes. (This feature of chiral packings has been discussed briefly in section 4.14)... 

Other interfacial chemistries are found in juxtamem-brane domains of certain proteins that show a preferential interaction with specific lipids in their head group region. Important lipids involved in these interactions include the polyphosphate phosphatidylinositol lipids, cholesterol, gangliosides, and sphingomyelin. Interfacial chemistries play a role in the formation of microdomains and can determine the effective concentration of certain amphiphilic drugs in different membranes or even in different leaflets of the same membrane. 

Helices that form pores will be amphiphilic because it is more favorable to have situated in the inner side of the pore hydrophilic amino acid side chains, while the outer side of the pore represents a more favorable environment for hydrophobic amino acid side chains since these are in contact with lipids. Some authors point to the possibility that such a structure contains hydrogen bonds between amino acid residues and the main chain in order to compensate opposite charges and oppositely oriented dipoles. A comparison between the strength of different interactions in the structure of soluble and membrane proteins leads to the conclusion that because of the decreased strength of hydrophobic interactions and increased strength of electrostatic interactions (because of the reduced dielectric constant), the electrostatic interactions play the main role in stabilizing the structure of membrane proteins. ... 

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