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High-throughput screening of one-bead-one-compound peptide libraries using intact cells
Choi-Fong Cho1, Babak Behnam Azad, Leonard G Luyt
1Translational Prostate Cancer Research Group, University of Alberta , 5-142C Katz Group Building, 114th Street and 87th Avenue, Edmonton, AB, T6G 2E1 Canada.
ACS Combinatorial Science
|July 4, 2013
Summary
Researchers developed a method for efficiently screening one-bead-one-compound libraries to find peptide ligands that target cancer cells. This technique uses reversible cross-linking with the COPAS biosorter for faster and more accurate cell sorting.
Area of Science:
- Biochemistry
- Molecular Biology
- Biotechnology
Background:
- One-bead-one-compound (OBOC) combinatorial libraries are crucial for discovering peptide ligands targeting cell surface proteins in diseases like cancer.
- Screening live cells is ideal for recognizing cell surface proteins, but current methods are inefficient for large-scale analysis.
Purpose of the Study:
- To evaluate the Complex Object Parametric Analyzer and Sorter (COPAS) large particle biosorter for high-throughput screening of bead-bound cells.
- To develop an efficient method for sorting live, bead-bound cells using the COPAS instrument for OBOC library screening.
Main Methods:
- Screening of RGD-containing peptides against human cancer cells expressing αvβ3 integrin using OBOC libraries.
- Utilizing the COPAS large particle biosorter for cell sorting.
- Implementing a reversible cross-linking strategy to secure bead-bound cells during sorting.
Main Results:
- Standard sorting with the COPAS instrument caused rapid dissociation of bead-associated cancer cells.
- Reversible cross-linking of cells to beads enabled quick and accurate sorting of cell/bead mixtures.
- The developed method is compatible with mass spectrometry-based peptide sequence analysis.
Conclusions:
- The reversible cross-linking method enhances the efficiency and accuracy of OBOC library screening using the COPAS biosorter.
- This approach facilitates the rapid identification of novel peptide ligands targeting cell surface proteins in their native conformation.
- This technique holds promise for advancing cancer research and drug discovery.
