Lipid membranes surface structure

Early investigations of peptides in membrane model systems included studies of mel-letin 124,125 220 221 spectra and polarization properties. This water-soluble peptide is found to be structureless in solution at neutral pH but was sensitive to environmental change. The undecapeptide hormone, substance P, a member of the tackykinin family, was also found by Choo et a].1222 to be unstructured in solution at physiological pH and to aggregate at high pH or on interaction with charged lipids. These data were used as counter-evidence to a hypothesis that the membrane surface structured the peptide to facilitate interaction with the receptor. 

The most likely way for pardaxin molecules to insert across the membrane in an antiparallel manner is for them to form antiparallel aggregates on the membrane surface that then insert across the membrane. We developed a "raft"model (data not shown) that is similar to the channel model except that adjacent dimers are related to each other by a linear translation instead of a 60 rotation about a channel axis. All of the large hydrophobic side chains of the C-helices are on one side of the "raft" and all hydrophilic side chains are on the other side. We postulate that these "rafts" displace the lipid molecules on one side of the bilayer. When two or more "rafts" meet they can insert across the membrane to form a channel in a way that never exposes the hydrophilic side chains to the lipid alkyl chains. The conformational change from the "raft" to the channel structure primarily involves a pivoting motion about the "ridge" of side chains formed by Thr-17, Ala-21, Ala-25, and Ser-29. These small side chains present few steric barriers for the postulated conformational change. 

Gorter and Grendel in 1925 [527], drawing on the work of Langmuir, extracted lipids from RBC ghosts and formed monolayers. They discovered that the area of the monolayer was twice that of the calculated membrane surface of intact RBC, indicating the presence of a bilayer. This was the birth of the concept of a lipid bilayer as the fundamental structure of cell membranes (Fig. 7.1). 

Phospholipids are amphiphilic substances i.e. their molecules contain both hydrophilic and hydrophobic groups. Above a certain concentration level, amphiphilic substances with one ionized or polar and one strongly hydrophobic group (e.g. the dodecylsulphate or cetyltrimethylammonium ions) form micelles in solution these are, as a rule, spherical structures with hydrophilic groups on the surface and the inside filled with the hydrophobic parts of the molecules (usually long alkyl chains directed radially into the centre of the sphere). Amphiphilic substances with two hydrophobic groups have a tendency to form bilayer films under suitable conditions, with hydrophobic chains facing one another. Various methods of preparation of these bilayer lipid membranes (BLMs) are demonstrated in Fig. 6.10. 

In Gram-negative bacteria which are characterised by a rather complex cell envelope, the CM is also referred to as inner membrane to distinguish it from a second lipid bilayer, termed outer membrane (OM). The space between these two layers is called the periplasm (PP). In the periplasmic space, many proteins are found with a variety of functions. Some are involved in biosynthesis and/or export of cell wall components and surface structures (e.g. pili, flagellae,... 

The ssDNA was immobilized stronger and faster on the GC surface in the presence of the lipid membrane than on a bare GC surface and using milder conditions [61]. The lipid membrane enhanced the stabihty of ssDNA towards desorption from the GC surface [61,62]. Moreover, the adsorption of ssDNA on BLM induced a conductance enhancement due to (1) structural changes (i.e., defect sites) within the membrane and (2) the increase in negative surface charge density of the membrane. The charge of the phosphate groups of ssDNA induced an increase of cation concentration in the electrical double layer [63]. 

Thus, the fat globules are surrounded, at least initially, by a membrane typical of eukaryotic cells. Membranes are a conspicuous feature of all cells and may represent 80% of the dry weight of some cells. They serve as barriers separating aqueous compartments with different solute composition and as the structural base on which many enzymes and transport systems are located. Although there is considerable variation, the typical composition of membranes is about 40% lipid and 60% protein. The lipids are mostly polar (nearly all the polar lipids in cells are located in the membranes), principally phospholipids and cholesterol in varying proportions. Membranes contain several proteins, perhaps up to 100 in complex membranes. Some of the proteins, referred to as extrinsic or peripheral, are loosely attached to the membrane surface and are easily removed by mild extraction procedures. The intrinsic or integral proteins, about 70% of the total protein, are tightly bound to the lipid portion and are removed only by severe treatment, e.g. by SDS or urea. 

The construction of the eye is completely different. The outer layer of this mucosa consists of a tiny tear layer of lipids and water which covers a superficial epithelium closed by double layer lipid membranes of 30-70 nm size interconnected by tight jnnctions. Three to seven layers of epithelial cells cover the stromal structures of conjunctiva or cornea. The conjnnctival surface has interposed cells secreting small amonnts of mucin, the so-called goblet cells, which are typically missing within the corneal epithelinm. The regeneration of epithelial structnres is dne to the limbal stem cells located deep in the Vogt s crypts, for the cornea. 

The lipids and proteins of membranes are inserted into the bilayer with specific sidedness thus membranes are structurally and functionally asymmetric. Many membrane proteins contain covalently attached oligosaccharides. Plasma membrane glycoproteins are always oriented with the carbohydrate-bearing domain on the extracellular surface. 

A third important structural pattern involves extensive use of amphipathic helices that lie partially embedded in a membrane surface. For example, the blood lipoproteins are lipid particles partially coated by amphipathic helices (Chapter 21).200 201... 

Describe the structure of biological membranes and the characteristic functions of lipid-, protein-, and carbohydrate-containing components. Describe the differences between inner and outer membrane surfaces. 

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