9RXL
SARS-CoV-2 nucleocapsid C-terminal domain in complex with BCY00018176
Summary for 9RXL
| Entry DOI | 10.2210/pdb9rxl/pdb |
| Descriptor | BCY00018176, Nucleoprotein, 1-[3,5-bis(3-bromanylpropanoyl)-1,3,5-triazinan-1-yl]-3-bromanyl-propan-1-one, ... (5 entities in total) |
| Functional Keywords | bicyclic peptides, antibody mimic, elisa, lfia, diagnostic, viral protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 4 |
| Total formula weight | 35721.15 |
| Authors | Brear, P.,Lulla, A.,Dods, R.,Bezerra, G.A.,Hyvonen, M. (deposition date: 2025-07-11, release date: 2026-03-04) |
| Primary citation | Shamsabadi, A.,Creamer, A.,Sadler, C.J.,Abdelwahed, A.,Gaynor, K.U.,Demydchuk, Y.,Ivanova-Berndt, G.,Van Rietschoten, K.,Beswick, P.,Chen, L.,Arruda Bezerra, G.,Lulla, A.,Brear, P.,Hyvonen, M.,Skynner, M.J.,Stevens, M.M. Utilizing Constrained Bicyclic Peptides for In Vitro Diagnostics. Acs Nano, 2026 Cited by PubMed Abstract: Constrained bicyclic peptides () with high affinity for biological targets have emerged as potentially powerful therapeutic agents, particularly for the targeting of cancer receptors. However, their antibody-mimetic properties have yet to be explored for use in diagnostic immunoassays. These synthetically derived compounds serve as biorecognition scaffolds that allow for facile site-selective modification and large-scale production. A phage display screen against various constructs of the SARS-CoV-2 nucleocapsid (N) protein identified several molecules with binding affinities ranging from the micromolar to the low nanomolar range. These molecules were validated in the development of enzyme- and nanozyme-linked immunosorbent assays, as well as enzymatic and colorimetric nanoparticle-based lateral flow immunoassays (LFIA) for the detection of ultralow concentrations of the SARS-CoV-2 N protein. We envision that these moieties enable robust, cost-effective, and large-scale development of ultrasensitive biosensors for a diverse range of biomarkers by leveraging their high binding affinity, minimalistic scaffold, and synthetic accessibility. PubMed: 41685809DOI: 10.1021/acsnano.5c19041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
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