Affinity Selection from Synthetic Peptide Libraries Enabled by De Novo MS/MS Sequencing
peer-reviewed · International Journal of Peptide Research and Therapeutics · 2022
| Date | 2022-03-01 |
| Type | peer-reviewed |
| Venue | International Journal of Peptide Research and Therapeutics |
| Publisher | Springer Science and Business Media LLC |
| Contribution | review |
| DOI | 10.1007/s10989-022-10370-9 |
| Citations (OpenAlex) | 10 |
Abstract
Recently, de novo MS/MS peptide sequencing has enabled the application of affinity selections to synthetic peptide mixtures that approach the diversity of phage libraries (> 108 random peptides). In conjunction with ‘split-mix’ solid phase synthesis to access equimolar peptide mixtures, this approach provides a straightforward means to examine synthetic peptide libraries of considerably higher diversity than has been feasible historically. Here, we offer a critical perspective on this work, report emerging data, and highlight opportunities for further methods refinement. With continued development, ‘affinity selection–mass spectrometry’ may become a complimentary approach to phage display, in vitro selection, and DNA-encoded libraries for the discovery of synthetic ligands that modulate protein function.
Methods and tools
- Affinity selection-mass spectrometry: Perspective on affinity selection from synthetic peptide libraries of phage-like diversity, made possible because de novo MS/MS sequencing identifies the binders without a library index.
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