ArticleProceedings of the National Academy of Sciences of the United States of America2021
An in vivo selection-derived d-peptide for engineering erythrocyte-binding antigens that promote immune tolerance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 11 citations in OpenAlex.
- Red blood cell-hitchhiking fluorescent probe to promote intraoperative diagnosis of human ovarian tumor.Science advances · 2025Article
- Fabrication of cytotoxic mirror image nanopores.Nature communications · 2025Article
- Advances in Ultrahigh Throughput Hit Discovery with Tandem Mass Spectrometry Encoded Libraries.Journal of the American Chemical Society · 2023Review
- In-Cell Penetration Selection-Mass Spectrometry Produces Noncanonical Peptides for Antisense Delivery.ACS chemical biology · 2023Article
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Authors and funding
13 authors at 5 institutions in 1 country.
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Abstract
When displayed on erythrocytes, peptides and proteins can drive antigen-specific immune tolerance. Here, we investigated a straightforward approach based on erythrocyte binding to promote antigen-specific tolerance to both peptides and proteins. We first identified a robust erythrocyte-binding ligand. A pool of one million fully d-chiral peptides was injected into mice, blood cells were isolated, and ligands enriched on these cells were identified using nano-liquid chromatography-tandem mass spectrometry. One round of selection yielded a murine erythrocyte-binding ligand with an 80 nM apparent dissociation constant,
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