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Tape-forming peptides

Table 1 Magnitudes of molecular parameters and macroscopic properties of the aqueous solutions of the two de novo-designed self-assembling 3-tape forming peptides P -l and P -2 (Aggeli et al., 2001b)... [Pg.19]

Carrick, L.M., Aggeli, A., Boden, N., Fisher, J., Ingham, E., and Waigh, T.A. "Effect of ionic strength on the self-assembly, morphology and gelation of pH responsive beta-sheet tape-forming peptides". Tetrahedron 63(31), 7457-7467 (2007). [Pg.41]

As an illustration of the second approach to biosynthesis, the work of Boden et al. will be taken as an example. Again the first step is to identify an interesting motif to be incorporated in a molecule. The motif that they have focussed on is the P-sheet. By incorporating a sequence which facilitates the formation of this structure it becomes possible to form a peptide which spontaneously self-assembles into P-sheet tapes. In appropriate solvents these peptides can form gels whose rheological properties can then be controlled by external parameters such as pH. Thus, what they have termed rational design coupled with the peptide synthesiser may yield macromolecules with a specific set of controlled properties. [Pg.156]

The various ribbons presented above consist of amphiphilic molecules arranged in bilayers. The long axis of the molecules is perpendicular to the ribbon plane or slightly tilted from this direction. But ribbons or tapes can also be formed from the assembly of molecular rods oriented with their long axis parallel to the width of the ribbon. This is the case for some peptides that form extended /3-sheet tapes which stack to form chiral superstructures (Fig. 3) [73]. It is also the case for numerous gelators consisting of a central aromatic core and chiral cholesteryl saccharidic moieties on the sides, such as the porphyrin derivative shown in Fig. 4 [74]. Chirality effects in these... [Pg.182]

Aggeli A, Bell M, Boden N et al (1997) Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes. Nature 386 259-262... [Pg.164]

Aggeli, A., Bell, M., Boden, N., Keen, J. N., Knowles, P. F., McLeish, T. C., Pitkeathly, M., and Radford, S. E. (1997). Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes. Nature 386, 259-262. [Pg.118]

The use of self-assembling peptides is also explored beyond the medical, pharmaceutical, or cosmetics industry. Areas of interest are among others functional foods, electronics, functional coatings, and catalysis (but different from enzyme research). As an example, peptides can be designed to switch from a random coil-like primary structure organization into an a-helix or [3-sheet secondary structure with unique properties. Short peptides align to form [3-sheet tapes with different functionalities, for example, hydrophilic and hydrophobic on either side of the tape to form monolayer coatings (Boden et al., 1996). [Pg.6]

Figure 32 Hierarchically structured composite fibers formed by a hybrid process, combining self-assembly of polymer-peptide nanotapes with peptide-directed silicification. ( Organic hierarchy levels are classified as peptide-polymer conjugate (level I), nanotapes with single p-sheet core (level II) and double p-sheet core (level III). Composite hierarchy levels are specified as proto-composite tapes (level IV), proto-composite fibers (level V), and fiber bundles (level VI).) Adapted from Kessel, S. Thomas, A. Borner, H. G. Angew. Chem., Int. Ed. 2007, 46, 9023 and Kessel, S. Bomer, H. G. Macromol. Rapid Commun. 2008,29,419. Reprinted with permission from Bomer, H. G. Prog. Polym. Sci. 2009,34,811. Copyright 2009, Elsevier. ... Figure 32 Hierarchically structured composite fibers formed by a hybrid process, combining self-assembly of polymer-peptide nanotapes with peptide-directed silicification. ( Organic hierarchy levels are classified as peptide-polymer conjugate (level I), nanotapes with single p-sheet core (level II) and double p-sheet core (level III). Composite hierarchy levels are specified as proto-composite tapes (level IV), proto-composite fibers (level V), and fiber bundles (level VI).) Adapted from Kessel, S. Thomas, A. Borner, H. G. Angew. Chem., Int. Ed. 2007, 46, 9023 and Kessel, S. Bomer, H. G. Macromol. Rapid Commun. 2008,29,419. Reprinted with permission from Bomer, H. G. Prog. Polym. Sci. 2009,34,811. Copyright 2009, Elsevier. ...
The 24-residue peptide K24 related to the transmembrane domain of the IsK protein was found to readily form /3-sheet tapes in lipid bilayers. The same peptide formed stable transparent gels with methanol or 2-chloroethanol at a concentration of 3 g by the same type of organization [97]. TEM of the gels revealed entangled polymeric tapes of single molecule thickness (0.7 nm). The much shorter, de novo 11-residue peptide with primary sequence MeCO-Gln-Gln-Arg-Phe-Gln-Trp-Gln-Phe-Glu-Gln-... [Pg.113]

By the aid of a modified peptide synthesizer solutions of two moles of Boc- or Ddz-amino acid salts (sodium- or triethylammonium form) in tetrahydrofuran or dichloro-methane at —40 °C are mixed for 5 minutes with one mole of phosgene in the same solvent at —40 °C, controlled by the punched tape program of the synthesizer (Fig. 44). The solution of the symmetric anhydride is added at —40 C to the gel polymer, which is contained in the centrifugal reactor (see p. 75) and is allowed to warm up to the cooling water temperature level (9—13 C) of the reactor during the peptide synthesis period of 30 minutes. Since the mode of action of the centrifugal reactor renders it possible to perfuse an external IR flow cell with the reaction solution, we are in a position to monitor directly the quality of the symmetric anhydride and its consumption, watching the characteristic absorptions on 1,830 and 1,760 cm [71]. In several cases the symmetric anhydrides were isolated in crystalline or solid form for characterization (Table 6). [Pg.51]


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See also in sourсe #XX -- [ Pg.17 , Pg.18 , Pg.19 ]




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