ArticleJACS Au2026
Highly Pure Combinatorial Peptide Libraries by Resin-Enabled Catch and Release.
Article in JACS Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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13 authors.
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Abstract
For peptide-drug conjugate (PDC) development, high-quality peptide ligands with easy functionalization are essential. Combinatorial chemical peptide libraries are key for discovering high-affinity non-natural ligands, yet their utility has long been hindered by low-purity libraries that cause false positives. To address this, we developed an N-terminal cysteine-based dynamic catch-and-release (CbDCR) platform, leveraging its unique 1,2-aminothiol motif as a privileged handle for site-selective orthogonal conjugation, enabling efficient library purification while retaining a universal anchor for downstream functionalization. A recyclable 2-formylphenylboronic acid resin (2FPBA resin) was designed to catch and release N-terminal cysteine-containing peptides in a pH-responsive manner, eliminating the need for complex tags and providing simplicity, scalability, and high purification efficiency through optimized workflows. The platform effectively purifies SPPS-synthesized peptides, enriches N-terminal cysteine-containing peptides from protein lysates, supports high-purity split-and-pool library preparation, and integrates with microplate-based high-throughput workflows. Using a highly pure "RGD"-focused nonstandard library, high-affinity integrin αvβ6-targeting peptides were identified, and three peptide-radionuclide conjugates with potential diagnostic value for pancreatic cancer were constructed via N-terminal cysteine. Overall, CbDCR streamlines library purification, affinity screening, and conjugate construction, accelerating the development of high-value peptide ligands and PDCs.
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