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Hydrophobic segments

Detergents containing a 1,3-diene group in the hydrophobic segment. Facile chemical modification by a Dieis-Aider reaction with hydrophiiic dienophiies in aqueous solution [69]... [Pg.197]

Historically, after the development of oligopeptide-based vesicles, several groups developed and characterized vesicles using polypeptide hybrid systems consisting of polypeptide and synthetic polymer blocks [17-19]. Soon thereafter, vesicles formed entirely from polypeptides, such as poly(L-lysine)-h-poly(L-leucine) and poly(L-lysine)-h-poly(L-glutamate), were developed [20, 21]. This review will focus on recent developments in the formation of vesicles composed of polypeptide hybrid or polypeptide systems, as well as the potential promise of these systems as effective dmg delivery vehicles. A specific example of a polypeptide-based vesicle is shown in Fig. 1, where the hydrophobic segment is a-helical and the hydrophilic segment is a random coil. [Pg.120]

Fig. 1 Vesicle construct formed from poly(L-lysine)-i)-poly(L-leucme) polypeptides where the poly(L-leucine) block corresponds to the a-helical hydrophobic segments and the poly (L-lysine) block corresponds to the random coil hydrophilic segments. Note that this is one specific example and not all vesicle constructs have a-helical and random coil blocks. Moreover, the amphiphilic copolymer can be comprised of either a pure block copolypeptide or a macromolecule consisting of a polypeptide and another type of polymer. Adapted from [20] with permission. Copyright 2010 American Chemical Society... Fig. 1 Vesicle construct formed from poly(L-lysine)-i)-poly(L-leucme) polypeptides where the poly(L-leucine) block corresponds to the a-helical hydrophobic segments and the poly (L-lysine) block corresponds to the random coil hydrophilic segments. Note that this is one specific example and not all vesicle constructs have a-helical and random coil blocks. Moreover, the amphiphilic copolymer can be comprised of either a pure block copolypeptide or a macromolecule consisting of a polypeptide and another type of polymer. Adapted from [20] with permission. Copyright 2010 American Chemical Society...
Fig. 3. (A) Model of the proposed pore forming part of K channel subunits. Segments S5 and S6 are possibly membrane-spanning helices. The helices are connected by a hydrophobic segment H5 which may be tucked into the lipid bilayer [48]. H5 is flanked by two proline residues P. Adjacent to these proline residues are amino acid side chains ( ) important for external TEA binding [45,46]. Approximately halfway between these two proline residues are amino acid side chains ( ) affecting internal TEA binding [46,47] and K channel selectivity [48]. (B) Mutations are indicated which affect in Shaker channels external TEA (TEAe) or internal TEA (TEA,) binding. Concentrations of TEA for half block of the wild-type and mutant K channels are given at the right-hand side of the corresponding sequence. Data have been compiled from [45-47]. Fig. 3. (A) Model of the proposed pore forming part of K channel subunits. Segments S5 and S6 are possibly membrane-spanning helices. The helices are connected by a hydrophobic segment H5 which may be tucked into the lipid bilayer [48]. H5 is flanked by two proline residues P. Adjacent to these proline residues are amino acid side chains ( ) important for external TEA binding [45,46]. Approximately halfway between these two proline residues are amino acid side chains ( ) affecting internal TEA binding [46,47] and K channel selectivity [48]. (B) Mutations are indicated which affect in Shaker channels external TEA (TEAe) or internal TEA (TEA,) binding. Concentrations of TEA for half block of the wild-type and mutant K channels are given at the right-hand side of the corresponding sequence. Data have been compiled from [45-47].
A. Audibert, J. Lecourtier, L. C. Bailey, and G. Maitland. Use of polymers having hydrophilic and hydrophobic segments for inhibiting the swelling of reactive argillaceous formations (Tutilisation d un... [Pg.352]

Two forms of this enzyme are known, a membrane-bound form mainly found in microsomes of all cells and a soluble form present in red blood cells. Structurally, the soluble form with 275 amino acid residues lacks a hydrophobic segment at the NH2 terminus which is present in the membrane-bound enzyme with 300 amino acid residues. Both isoforms are produced by a single gene on chromosome 22 (T17,Y4). [Pg.33]

Hard contact lenses are composed of a polymer that repels water because the constituent repeating units (the monomers that link together to form the polymer) are nonpolar, hydrophobic segments. The first hard contact lens was constructed in 1948 from the monomer known as methyl methacrylate (MMA), yielding the polymer poly(methyl methacrylate) or PMMA. This material offers durability, optical transparency, and acceptable wettability for optimal comfort. Today the rigid lens material of hard contact lenses is often constructed by combining MMA with one or more additional hydrophobic monomers to provide better gas permeability. [Pg.221]

Recently, many studies have focused on self-assembled biodegradable nanoparticles for biomedical and pharmaceutical applications. Nanoparticles fabricated by the self-assembly of amphiphilic block copolymers or hydrophobically modified polymers have been explored as drug carrier systems. In general, these amphiphilic copolymers consisting of hydrophilic and hydrophobic segments are capable of forming polymeric structures in aqueous solutions via hydrophobic interactions. These self-assembled nanoparticles are composed of an inner core of hydrophobic moieties and an outer shell of hydrophilic groups [35, 36]. [Pg.37]

The solubility parameter of water is 17 or 23, depending on the association structure of water used in the calculation. None of the values listed in Table II are within two units of either value and by the general rules of the solubility concept, none of the polymers in Table II should be water soluble. Homopolymers of monomers c, e, or f in Figure 3 are not water soluble. The solubility values listed for the W-SPs studied do not correlate with the equilibrium pressures observed. A general correlation is noted if the values of the most hydrophobic segments (i.e., the oxypropyl, oxybutyl and acetate) are compared with PMVE. The... [Pg.121]

The differences in time-dependent adsorption behavior between 99% PVAC at 25° and 50°C demonstrate the influence of intra- and intermolecular hydrogen bonding in the adsorption process. The limiting surface pressure of the hydrophobic water-soluble polymer appears to be 33 mN/m, approximately 7 mN/m below that of commonly used surfactants. The rate of attainment of equilibrium surface pressure values is faster if there is uniformity of the hydrophobic segments among the repeating units of the macromolecule. [Pg.127]

Integral membrane proteins with one transmembrane domain may have soluble domains at either or both surfaces. An example of a monotopic protein, cytochrome b5 has a single hydrophobic segment that forms a hairpin loop, acting as an anchor to the cytoplasmic surface but probably not totally penetrating the bilayer. [Pg.24]

The transmembrane domain in the RPTK is a hydrophobic segment of 22-26 amino acids inserted in the cell membrane. It is flanked by a proline-rich region in the N-terminus and a cluster of basic amino acids in the C-ter-minus. This combination of structures secures the transmembrane domain within the lipid bilayer. There is a low degree of homology in the transmembrane domain, even between two closely related RPTKs, suggesting that the primary sequence contains little information for signal transduction. [Pg.422]

As discussed in the preceding sections, fluid, globular micelles are formed from monoalkyl surfactants, whereas the liquid-crystalline bilayer structure is formed from a variety of dialkyl amphiphiles and from single-chain amphiphiles with rigid hydrophobic segments. It may then be asked what structure is expected from amphiphiles with three alkyl chains. [Pg.439]

Sakaguchi, M., Tomiyoshi, R., Kuroiwa, T., Mihara, K., and Omura, T. (1992). Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment. Proc. Natl Acad. Sci. U.S.A. 89, 16-19. [Pg.341]


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See also in sourсe #XX -- [ Pg.62 ]

See also in sourсe #XX -- [ Pg.52 ]




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Hydrophilic and hydrophobic segments)

Hydrophobic segments biodegradable

Poly hydrophobic segments

Polymer micelles hydrophobic segments

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