Polypeptides amphiphilic structures

This polypeptide is structurally identical to ABA-type triblock copolymer with a central hydrophdic elastomeric end-block capped with two hydrophobic plastic end-blocks and exhibits amphiphilic characteristics. The end-blocks of the polymer were chosen in such a way that their LCST would reside at or near room temperature. Thus the polymer exhibits phase separation, which is analogue to conventional TPEs, and offers TPE gels under physiological relevant conditions [104]. Glutamic acid residue is placed periodically in the elastomeric mid-block to increase its affinity towards the aqueous... 

In nature, polypeptides with amphiphilic structures are known to form transmembrane channels formed by an assembly of several helices, so as to present their polar faces inward and their apolar faces outward. In view of such behavior, the photochromic amphiphilic polypeptide was incorporated into a cationic bilayer membrane composed of dipalmitoyl phosphatidyl choline.11201 Fluorescence and microscopic measurements provided evidence that the polypeptide was able to form bundles of helical molecules analogous to their natural counterparts, which acted as transmembrane channels for K+ ions. Irradiation, and the consequent transacts isomerization of the azobenzene link, caused a bending of the molecular structure and a destabilization of the transmembrane bundles. Therefore, formation of ion permeable channels would be favored or inhibited depending on whether the azo moiety... 

The major casein monomer subunits have random coil conformation that facilitates strong protein-protein interaction via hydrophobic and ionic bonding. The unique amphiphilic structure, which arises from separately clustered hydrophobic and negatively charged (acidic and ester phosphate) amino acid residues along the polypeptide chain, makes them susceptible to pH and Ca ion concentration effects. This amphiphilic nature is probably responsible for the excellent surfactant properties of commercial caseinate in a variety of food applications. 

Fig. 5 Polypeptide vesicles demonstrate the ability to utilize the EPR effect, (a) Chemical structure of the amphiphilic block polypeptide PSar-b-PMLG. (b) Fluorescence image using fluorescently labeled PEG. Fluorescence is not observed in the cancer site although accumulation is observed in the bladder, (c) Fluorescence image using ICG-labeled vesicles, showing evidence of vesicle accumulation due to the EPR effect. Adapted from [41] with permission. Copyright 2008 American Chemical Society...

Polymeric phospholipids based on dioctadecyldimethylammonium methacrylate were formed by photopolymerization to give polymer-encased vesicles which retained phase behavior. The polymerized vesicles were more stable than non-polymerized vesicles, and permeability experiments showed that vesicles polymerized above the phase transition temperature have lower permeability than the nonpolymerized ones [447-449]. Kono et al. [450,451] employed a polypeptide based on lysine, 2 aminoisobutyric acid and leucine as the sensitive polymer. In the latter reference the polypeptide adhered to the vesicular lipid bilayer membrane at high pH by assuming an amphiphilic helical conformation, while at low pH the structure was disturbed resulting in release of the encapsulated substances. 

The investigation was then extended to a monolayer formed from dipalmitoyl phosphatidyl choline and the same amphiphilic photochromic polypeptide XXIII.11211 When the monolayer was kept in the dark, the polypeptide molecules arranged themselves perpendicularly to the membrane (the water/air interface) and formed a bundle of helices which could be observed by atomic force microscopy as a transmembranous particle of about 4 nm in diameter. Irradiation with UV light and the consequent trans—>tis isomerization of the azobenzene moiety caused a bending of the molecular main chain, which in turn produced a destabilization and dena-turation of the bundle of helices in the monolayer. After removal of the light, the polypeptide molecules reverted to their original bundle structure. 1211... 

Davis, J. H., dare, D. M., Hodges, R. S., and Bloom, M. (1983). Biochem. 22, S298-S30S. Structure of a synthetic amphiphilic polypeptide and lipids in a bilayer structure. 

This review covers the literature on the aggregation of (homo)polypeptide hybrid copolymers and copolypeptides in dilute solution, which was published up to June 2005 a recent review on amphiphiles consisting of peptide sequences is given elsewhere in [12]. It was a particular concern to give a comprehensive overview on secondary structure effects in the self-assembly of these copolymers. Briefly presented are also structures in concentrated solutions (lyotropic phases) and in heterophase systems (see also [14]). 

A new polymeric amphiphile based on cationic poly(L-lysine), which was partially modified with hydrophobic palmitoyl chains and hydrophilic neutral methoxy-poly(ethylene glycol) (Fig. 7e), was introduced by Uchegbu et al. [38,39], In water in the presence of cholesterol, these copolymers assembled into vesicles with diameters ranging from 200 to 600 nm (DLS, freeze-fracture TEM), depending on the chemical composition of the copolymer and the length of the polypeptide backbone. More detailed information about the secondary structure of chains and the structure of vesicle membranes were not given. 

Surface-active materials consist of molecules containing both polar and nonpolar portions, i.e., amphiphilic molecules. The proteins are typically amphiphilic, polymeric substances made of amino acid residues combined in definite sequences by peptide bonds (primary structure). In many cases polypeptide chains are present in helical or /3-sheet configuration (secondary structure) which are stabilized by intramolecular (S-S and hydrogen) bonding. The next structural level, the tertiary structure, is determined by the folding of the polypeptide chains to more or less compact globules, maintained by hy-... 

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