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Bait peptides

Fig. 34 Functionalisation of bait peptides. I Gold-labelled streptavidin is attached directly. 2 Biotin-labelled anti-FLAG antibody is bound to the FLAG on the peptide (reaction b) and this is used to attach gold-labelled streptavidin (reaction d). Reprinted with permission from Ryadnov and Woolfson [76]. Copyright 2004 American Chemical Society... Fig. 34 Functionalisation of bait peptides. I Gold-labelled streptavidin is attached directly. 2 Biotin-labelled anti-FLAG antibody is bound to the FLAG on the peptide (reaction b) and this is used to attach gold-labelled streptavidin (reaction d). Reprinted with permission from Ryadnov and Woolfson [76]. Copyright 2004 American Chemical Society...
A 17 amino acid long peptide sequentially related to opioid peptides in particular dynorphin A. OFQ/N is inactive at the 5, k, and p opioid receptors, but binds to its own NOP receptor (formerly ORL-1, for opioid receptor like-1). In contrast to opioid peptides, OFQ/N has no direct analgesic properties. OFQ/N is the first example for the discovery of a novel neurotransmitter from tissue extracts by using an orphan receptor as bait. Centrally administered in rodents, OFQ/N exerts anxiolytic properties. OFQ/N agonists and antagonists... [Pg.917]

Figure 28.19 The cleavage reaction of FeBABE involves a catalytic process using peroxide and ascorbate to form reactive oxygen species. Any protein structure in the immediate vicinity of the FeBABE label on the bait protein will undergo peptide bond cleavage. Figure 28.19 The cleavage reaction of FeBABE involves a catalytic process using peroxide and ascorbate to form reactive oxygen species. Any protein structure in the immediate vicinity of the FeBABE label on the bait protein will undergo peptide bond cleavage.
In a more modified approach, differential display proteomics can also be done with no separation of proteins. This is called the protein chip approach. In this method, a variety of bait proteins such as antibodies, peptides, or protein fragments may be immobilized in an array format on specially treated surfaces. The surface is then probed with the samples of interest. Proteins that bind to the relevant target can then be analyzed by direct MALDI readout of the bound material (Nelson, 1997 Davies et ah, 1999). Lor example, well-characterized antibodies can be used as bait. Protein samples from two different cell states are then labeled by different fluorophores, mixed together, and used as probe. In such a case, the fluorescent color acts as an indicator for any change in the abundance of the protein that remains bound to the chip (Lueking et ah, 1999). A number of technical problems would still need to be overcome before applying this technique for large-scale analysis of proteins. [Pg.80]

Proteomic Identification of GIPs Associated With 5-HT2C and 5-HT2A Using Short C-Terminal Peptides as Bait... [Pg.245]

We screened peptides that recognize and bind to a partial structure of DCMU from a combinatorial library of tetrapeptides on solid-phase. We used the 3,4-dichloroaniline (DCA) group as bait after taking into consideration the chemical structure of DCMU and its simple synthesis. To screen peptides that bind to the DCA group, a fluorescent-labeled dichloroaniline molecule (NBD-DCA) was synthesized by conjugating a dye with the dichloroaniline through a linker (Fig. 8.4). We selected a NBD moiety for the dye because of its small chemical structure and large Stokes shift. [Pg.209]

Protein micro-arrays equipped with specific capture molecules such as antibodies, fragments thereof, peptides, or other bait molecules have been developed in recent years [37, 38]. Here, the challenges lay not only in the generation of libraries of cap-... [Pg.1329]

The yeast two-hybrid system detects protein-protein or protein-peptide interactions in vivo. The target or bait protein and the ligand library are fused to either the DNA-binding domain or the transcription activation domain. Yeast cells are transformed with both plasmids and only the transformants expressing the protein-ligand interaction are selected (Y2). The main advantage is the one-step in vivo screening however, the library size is limited to about lO because of the transformation efficiency of the cells. [Pg.229]


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