Ligand-regulated peptide aptamers

The peptide aptamer approach employs high-throughput selection to identify members of a randomized peptide library displayed from a scaffold protein by virtue of their interaction with a target molecule. Extending this approach, we have developed a peptide aptamer scaffold protein that can impart sm...

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Vydáno v:Methods in molecular biology (Clifton, N.J.) Ročník 535; s. 315
Hlavní autor: Miller, Russell A
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States 2009
Témata:
Aptamers, Peptide - chemistry
Aptamers, Peptide - genetics
Aptamers, Peptide - metabolism
Ligands
Peptide Library
Protein Binding
Protein Structure, Tertiary
SELEX Aptamer Technique - methods
Sirolimus - metabolism
Two-Hybrid System Techniques
ISSN:1064-3745
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Shrnutí:The peptide aptamer approach employs high-throughput selection to identify members of a randomized peptide library displayed from a scaffold protein by virtue of their interaction with a target molecule. Extending this approach, we have developed a peptide aptamer scaffold protein that can impart small-molecule control over the aptamer-target interaction. This ligand-regulated peptide (LiRP) scaffold, consisting of the protein domains FKBP12, FRB, and GST, binds to the cell-permeable small-molecule rapamycin and the binding of this molecule can prevent the interaction of the randomizable linker region connecting FKBP12 with FRB. Here we present a detailed protocol for the creation of a peptide aptamer plasmid library, selection of peptide aptamers using the LiRP scaffold in a yeast two-hybrid system, and the screening of those peptide aptamers for a ligand-regulated interaction.
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ISSN:1064-3745
DOI:10.1007/978-1-59745-557-2_18