Peptide interactions, phospholipid membranes/surfaces

The arrangement of the proteins within the membrane seems to depend to some extent on the electrostatic surface potential and interface permittivity. It is influenced by electrostatic interaction between the proteins, polar head groups of the phospholipid and ions within the aqueous medium of the membrane surface. This can be affected by exogenous molecules such as drugs. Phospholipid-induced conformational change in intestinal calcium-binding protein in the absence and presence of Ca2+ has been described [37]. There is, however, no doubt that hydrophobic interactions between peptides and membrane interfaces play an important role. A general frame-... 

These results show that the ability of these signal peptides to interact with phospholipid monolayers indeed correlates with their in vivo activity. The pressure increases due to the functional signal peptides (8—11 dyn/cm) are in the same range as those caused by proteins known to insert into monolayers (Bougis et al., 1981). In contrast, prothrombin, which binds only to the membrane surface, causes a pressure increase in a phospholipid monolayer of 1.9-2.3 dyn/cm (Mayer et al., 1983). These values are almost identical to those obtained for perturbation of the monolayer by the deletion-mutant signal peptide. 

Protein and peptide interactions with phospholipid membranes and surfaces... 

Interest in protein and peptide interactions with phospholipid membranes and surfaces originates from its importance for both key biophysical processes (eg, atherosclerosis, Alzheimer s, and other plaque-related diseases) and a wide range of biomedical applications. For example, control of protein/peptide adsorption allows reduction of inflammation and other unwanted biopharmaceutical effects in phospholipid-based biomaterials and dmg delivery but also improved signal-to-noise in biosensors and... 

Although issues thus remain with simpler aspects of protein/peptide interactions with phospholipid membranes, there has been a clear shift in the past few years to more complex membranes, notably those containing key nonlipid membrane components such as LPS, Upoteichoic acid, and proteoglycans. Protein/peptide interactions with such LPSs are important in various biological contexts, including Upoprotein deposition at proteoglycan-covered endothelial surfaces in atherosclerosis, lectin... 

Huang P, Loew GH (1995) Interaction of an amphiphilic peptide with a phospholipid bilayer surface by molecular dynamics simulation study. J Biomol Struct Dyn 12(5) 937-956 Bemeche S, Nina M, Roux B (1998) Molecular dynamics simulations of melittin in a dimy-ristoylphosphatidylcholine bilayer membrane. Biophys J 75(4) 1603 1618 Woolf TB, Roux B (1994) Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer. PNAS 91(24) 11631 11635... 

Thus, the efficiency of energy transfer between donors and acceptors randomly distributed in a plane depends on R0, a, and a, and the transfer efficiency is independent of a. The important point was made that surface density of the acceptor could be 1 per 500 phospholipids for R0 > 30 A. Using these equations for different donor and acceptor concentrations, the data were matched against the different theoretical curves to obtain the R0. An example of the application of the method of Fung and Stryer(81) is the study of energy transfer between the tryptophan of a membrane protein (or peptide models of proteins) and DPH,(83) in which it was shown that efficient energy transfer can occur without any special interaction being required between DPH and the proteins in specific areas of the membrane. 

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