Peptides and peptidomimetics have been of attractive agents that can capture macrobiolecules such as proteins, polysaccharides, lipids, and nucleic acids with a great deal of affinity and specificity. Taking advantages of bead-based libraries, associated with easy generation of vast diversity, many groups have approached to developing high throughput screening technologies on this useful platform for the last two decades. However, it is now a wide consensus that dealing with the bead-based libraries for screening against biologically relevant target objects are not obviously performed in association with the residual non-specific interactions and lack of reproducibility from batch to batch. High occurrence of false positives often perturbs the sorting process and makes the entire screening campaign hardly reliable. Hence, we have assessed and demonstrated several ways to tackle these issues by optimizing the structure and the property of the libraries as well as by introducing more orthogonal type of fluorescence probe for labeling the target biomarker. As a consequence the results are considerably more reliable and reproducible to generate sustainable short peptide ligands, of which affinity and specificity are validated by surface plasma resonance (SPR) and dot blot experiments. These findings may open a new chapter to practical applications of bead-based libraries for high throughput screening. The developed agents, highly potent and specific, may eventually replace antibody to capture biomarkers of clinical importance.

Optimization of bead-based peptide libraries toward more reliable screenings

248th National Meeting (2014)

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