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Libraries combinatorial peptide

SI Cho, W Zheng, A Tropsha. Rational combinatorial library design 2. Rational design of targeted combinatorial peptide libraries using chemical similarity probe and the inverse QSAR approaches. J Chem Inf Comput Sci 38 259-268, 1998. [Pg.368]

Donia, M.S., Hathaway, B.J., Sudek, S. et al. (2006) Natural combinatorial peptide libraries in cyanobacterial symbionts of marine ascidians. Nature Chemical Biology, 2, 729. [Pg.260]

Figure 16.4 Graph depicting the percentage of lysine residues among peptides that bind to the indicated monoclonal antibodies. The peptides were isolated after affinity selection (biopanning) from a phage-displayed combinatorial peptide library. The peptides are grouped as to whether they are susceptible to formalin fixation, resulting in a loss of immunoreactivity. Figure 16.4 Graph depicting the percentage of lysine residues among peptides that bind to the indicated monoclonal antibodies. The peptides were isolated after affinity selection (biopanning) from a phage-displayed combinatorial peptide library. The peptides are grouped as to whether they are susceptible to formalin fixation, resulting in a loss of immunoreactivity.
Scheme 10.5 Peptide encoded combinatorial peptide libraries via enzyme-mediated spatial segregation. P-P. Substrate with a scissile bond between P and P, S. Terminal Residue of the screening structure, C. Terminal Residue of the coding structure. Scheme 10.5 Peptide encoded combinatorial peptide libraries via enzyme-mediated spatial segregation. P-P. Substrate with a scissile bond between P and P, S. Terminal Residue of the screening structure, C. Terminal Residue of the coding structure.
Huang, P.Y. and Carbonell, R.G., Affinity chromatographic screening of soluble combinatorial peptide libraries, Biotechnol. Bioeng., 63, 633-641, 2000. [Pg.382]

Fig. 6 Dynamic combinatorial peptide library that expioits enzyme reactions to control self-assembly processes under thermodynamic controi. (a) Emergence of the potentiai peptide derivatives of varying length in a library of interconverting molecules formed from the staring materials of Fmoc L/L2 system. Fmoc-Ls is preferentially formed. Corresponding AFM images of the fibrillar structures formed at 5 min after the addition of enzyme, and the sheet-like structures observed after 2000 h show that redistribution of the derivatives is accompanied by the remodelling from fibres (Fmoc L3) to sheet-like structures (Fmoc L5). (b) HPLC analysis of the composition of the system reveals the formation and the stabilisation of Fmoc-Ls over time. Modified from [21]... Fig. 6 Dynamic combinatorial peptide library that expioits enzyme reactions to control self-assembly processes under thermodynamic controi. (a) Emergence of the potentiai peptide derivatives of varying length in a library of interconverting molecules formed from the staring materials of Fmoc L/L2 system. Fmoc-Ls is preferentially formed. Corresponding AFM images of the fibrillar structures formed at 5 min after the addition of enzyme, and the sheet-like structures observed after 2000 h show that redistribution of the derivatives is accompanied by the remodelling from fibres (Fmoc L3) to sheet-like structures (Fmoc L5). (b) HPLC analysis of the composition of the system reveals the formation and the stabilisation of Fmoc-Ls over time. Modified from [21]...
While in normal combinatorial peptide libraries (either chemical or phage display) each component has a unique sequence that is different from all others, in the cycloscan libraries all components have the same sequence, but differ in their conformation. This conformational diversity is generated in a dendrimeric hierarchy as shown exemplarily in Scheme 27 for the parent linear heptapeptide A-B-C-D-E-F-G. The diversity of the 1st order sublibrary (this nomenclature was adopted from Furka[468l) is based on the mode of cyclization. Excluding the head-to-tail cyclization there are seven different modes of cyclization that can be used for cycloscan three natural modes of cyclization and four modes of N-backbone cyclization. In addition there are five theoretical modes of C-backbone cyclization (see Scheme 1) which are not included in Scheme 27. [Pg.515]

Figure 8. Selection of the phage from the phage-displayed combinatorial peptide library [9]... Figure 8. Selection of the phage from the phage-displayed combinatorial peptide library [9]...
For some applications it might be desirable to cleave the product from a support in two or more portions. This can be realized by derivatizing a functionalized support with a mixture of different linkers that enable a sequential cleavage [9]. The resulting support can, for instance, be used to prepare and screen combinatorial peptide libraries by the mix-and-split method ([10-12] one different peptide on each bead). The first portion of peptide released would be tested for biological activity, and, once an active peptide had been identified, the remaining peptide on the support could be used for structure elucidation. [Pg.40]

Using the Coiled-Coil Template for Conformationally Defined and Constrained Combinatorial Peptide Libraries... [Pg.97]

Synthesis of the C-Terminal Fragment for Combinatorial Peptide Libraries General Procedure 1117 ... [Pg.99]

Screening combinatorial peptide libraries with intact cells is a rapid way of discovering cell surface-binding ligands.22 25 The procedure is divided into three sections (1) preparation and sterilization of the bead library,... [Pg.312]

Radionuclide-based screening for protein kinase substrates is a quick and effective method for determining peptide substrates for protein kinases.28-31 The method presented here is based on the screening of random synthetic combinatorial peptide libraries with a protein kinase and is divided into two main parts (1) the phosphorylation of the peptide bead library and (2) the recovery and characterization of positive beads. [Pg.315]

Youngquist, R. S. Fuentes, G. R. Lacey, M. E Keough, T. 1995. Generation and screening of combinatorial peptide libraries designed for rapid screening by mass spectrometry. J. Am. Chem. Soc., 117, 3900-3905. [Pg.233]

S Cabilly. The basic structure of filamentous phage and its use in the display of combinatorial peptide libraries. Mol Biotechnol 12 143-148, 1999. [Pg.534]

R Hyde-DeRuyscher, LA Paige, DJ Christensen, N Hyde-DeRuyscher, A Lim, ZL Fredericks, J Kranz, P Gallant, J Zhang, SM Rocklage, DM Fowlkes, PA Wendler, PT Hamilton. Detection of small-molecule enzyme inhibitors with peptides isolated from phage-displayed combinatorial peptide libraries. Chem Biol 7 17-25, 2000. [Pg.534]

Recently, the enrichment of proteins by a combinatorial peptide library allowed demonstrating quite easily the presence or the absence of proteins, for instance, in almond s milk and orgeat syrup (65), in coconut milk (66), in a cola drink (67), in ginger ale (68), and even in white wine vinegar that is not really a beverage (69) (see in the succeeding text). [Pg.146]


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Combinatorial libraries, peptide-based

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Combinatorial peptide library electrospray mass spectrometry

Combinatorial peptide library materials

Combinatorial peptide library phage display

Combinatorial peptide library solid-phase synthesis

Combinatorial peptides

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Peptide combinatorial library applications

Peptide combinatorial library assay

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