Peptide combinatorial

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. 

G. Jung (ed.), Combinatorial Peptide and Nonpeptide Libraries. A Handbook, VCH, Weinbeim, 1996. 

Polymerase Chain Reaction (LLNL, Idaho Tech, Cepheid) Combinatorial Peptides (University of Texas)... 

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. 

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.

Combinatorial Peptide and Non-peptide Libraries, ed. G. Jung, VCH, Weinheim, Germany, 1996. 

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.

Lowe et al. investigated the substrate selectivity of the proteases papain and chy-motrypsin using PEGA-bound combinatorial peptide hbraries (32) (Fig. 10.3) [24]. The quahtative extent of enzymatic cleavage of the resin-bound peptide in case of an accepted substrate strand was rapidly visualized by a significant reduction in the fluorescence of the beads visuahzed with a fluorescence microscope. Furthermore it was proven that substrate selectivity of the enzyme remain the same on the solid phase and in solution. 

Huang, P.Y. and Carbonell, R.G., Affinity chromatographic screening of soluble combinatorial peptide libraries, Biotechnol. Bioeng., 63, 633-641, 2000. 

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. 

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. 

Using the Coiled-Coil Template for Conformationally Defined and Constrained Combinatorial Peptide Libraries... 

Synthesis of the C-Terminal Fragment for Combinatorial Peptide Libraries General Procedure 1117 ... 

FACS Screening of Combinatorial Peptide and Protein Libraries Displayed on the Surface of Escherichia coli Cells... 

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