ArticleProceedings of the National Academy of Sciences of the United States of America2002
Stable "zeta" peptides that act as potent antagonists of the high-affinity IgE receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 49 citations in OpenAlex.
- MOrPH-PhD: A Phage Display System for the Functional Selection of Genetically Encoded Macrocyclic Peptides.Methods in molecular biology (Clifton, N.J.) · 2022Article
- MOrPH-PhD: An Integrated Phage Display Platform for the Discovery of Functional Genetically Encoded Peptide Macrocycles.ACS central science · 2020Article
- Fifty years later: Emerging functions of IgE antibodies in host defense, immune regulation, and allergic diseases.The Journal of allergy and clinical immunology · 2016Review
- Accelerated dissociation of IgE-FcεRI complexes by disruptive inhibitors actively desensitizes allergic effector cells.The Journal of allergy and clinical immunology · 2014Article
- An IgE receptor mimetic peptide (PepE) protects mice from IgE mediated anaphylaxis.Molecular bioSystems · 2013Article
- IgE and mast cells in allergic disease.Nature medicine · 2012Review
- Fc receptor-targeted therapies for the treatment of inflammation, cancer and beyond.Nature reviews. Drug discovery · 2012Review
- Selection of peptides that target the aminoacyl-tRNA site of bacterial 16S ribosomal RNA.Biochemistry · 2009Article
- Identification of cyclic peptides able to mimic the functional epitope of IgG1-Fc for human Fc gammaRI.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009Article
- Computer applications for prediction of protein-protein interactions and rational drug design.Advances and applications in bioinformatics and chemistry : AABC · 2009Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently we described a family of peptides, unrelated in sequence to IgE, that form stable beta-hairpins in solution and inhibit IgE activity in the microM range [Nakamura, G. R., Starovasnik, M. A., Reynolds, M. E. & Lowman, H. B. (2001) Biochemistry 40, 9828-9835]. Using an expanded set of peptide-phage libraries, we found a simpler motif, X(2)CPX(2)CYX, for binding to the high-affinity IgE receptor. In solution, one of these peptides spontaneously formed a covalent antiparallel dimer. We subsequently linked these monomers in a single-chain construct on phage and optimized receptor binding. Ultimately, peptides with 30 nM affinity were produced. NMR studies showed that the peptide adopts a stable fold consisting of two "zeta" (zeta)-shaped moieties. Structure-activity analyses reveal a single binding site created by the zeta-dimer, with two tyrosine residues important for structural stability and two proline residues important for Fc epsilon RI binding. The peptides inhibit histamine release from cultured cells and are extremely stable in biological fluids. The zeta peptides appear to act as competitive IgE inhibitors and suggest possibilities for design of novel IgE antagonists.
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