Nature Biotechnology23, 746 - 751 (2005)
Published online: 22 May 2005; | doi:10.1038/nbt1099
A high-throughput assay for assessing the cell permeability of combinatorial libraries
Peng Yu1, 2, Bo Liu1, 2
& Thomas Kodadek1
1
Departments of Internal Medicine and Molecular Biology and the Center for Biomedical Inventions, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, Texas 75390-8573, USA.
There is great interest in the identification of synthetic molecules that are capable of manipulating protein-protein interactions in living cells. Peptides, unlike other classes of small molecules, have binding properties appropriate for this application, but most are poorly cell permeable and sensitive to proteases. Therefore, considerable effort has been expended in the development of libraries of oligomeric peptide-like molecules1,
2,
3,
4. However, there are no clear-cut rules to guide the design of libraries rich in cell permeable compounds. Furthermore, currently available empirical methods to assess permeability may not accurately reflect true permeability and/or are capable of only modest throughput5,
6,
7,
8,
9,
10,
11,
12. We describe here an assay for assessing the relative cell permeability of synthetic molecules in the context of steroid fusions that is capable of high throughput and can be used in any transfectable cell line.
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