Isolation of protein ligands from large peptoid libraries.

J Am Chem Soc

Center For Biomedical Inventions, Departments of Internal Medicine and Molecular Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-8573, USA.

Published: November 2003

AI Article Synopsis

  • The isolation of protein-binding ligands is a key aim in the field of proteomics, which studies proteins and their functions.
  • Traditional native peptides can be problematic due to their vulnerability to proteases, making them less suitable for certain uses.
  • The authors present the development of diverse combinatorial libraries of peptoids, which are suggested to be an affordable and effective alternative for sourcing protein ligands.

Article 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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Source
http://dx.doi.org/10.1021/ja036417xDOI Listing

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