Literature DB >> 14611236

Isolation of protein ligands from large peptoid libraries.

Prasanna G Alluri1, M Muralidhar Reddy, Kiran Bachhawat-Sikder, Hernando J Olivos, Thomas Kodadek.   

Abstract

The isolation of ligands for large numbers of proteins is an important goal in proteomics. Whereas peptide libraries are rich sources of protein-binding molecules, native peptides have certain undesirable properties, such as sensitivity to proteases that make them less than ideal for some applications. We report here the construction and characterization of large, chemically diverse combinatorial libraries of peptoids (N-substituted oligoglycines). A protocol for the isolation of specific protein-binding molecules from these libraries is described. These data suggest that peptoid libraries will prove to be inexpensive and convenient sources of protein ligands.

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Year:  2003        PMID: 14611236     DOI: 10.1021/ja036417x

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  81 in total

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9.  A reversible and highly selective inhibitor of the proteasomal ubiquitin receptor rpn13 is toxic to multiple myeloma cells.

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10.  Aβ42-binding peptoids as amyloid aggregation inhibitors and detection ligands.

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