10SE
The CryoEM structure of T8 nanofiber
Summary for 10SE
| Entry DOI | 10.2210/pdb10se/pdb |
| EMDB information | 75432 |
| Descriptor | T8 nanofiber, OCTANOIC ACID (CAPRYLIC ACID) (2 entities in total) |
| Functional Keywords | nanofiber, protein fibril |
| Biological source | synthetic construct More |
| Total number of polymer chains | 18 |
| Total formula weight | 21860.59 |
| Authors | |
| Primary citation | Godbe, J.M.,Zhang, H.,Sharma, A.K.,Ernst, K.N.,Jing, Z.,Dyer, M.R.,Prior, J.L.,Teubner, E.,Manion, B.,Tang, R.,Yang, Y.,Shokeen, M. Tailoring Avidity through Morphology: Structure-Avidity Relationship in CD38-Binding Nanofiber Radiotracers. Acs Appl Bio Mater, 9:4242-4257, 2026 Cited by PubMed Abstract: The lack of targeted molecular imaging agents for multiple myeloma (MM) hinders precise disease characterization and theranostic development. We address this by engineering a tunable platform of self-assembled peptide nanofibers that target CD38, a key antigen in MM. Simple variation of a conjugated lipid tail length (C4-C12) dictates the supramolecular architecture, as revealed by high-resolution cryo-EM. This structural control directly modulates biological function: avidity for CD38 increases monotonically with tail length, culminating in T12 nanofibers with sub-nanomolar affinity. This optimized morphology also enables unique pH-responsive di-tyrosine cross-linking and, critically, facilitates polyvalent cell-surface engagement that outcompetes high-affinity monomers in vitro. The nanofibers are efficiently radiolabeled with Cu, exhibit exceptional serum stability, and show no toxicity at doses 20-fold above projected imaging use. By establishing lipid tail length as a simple, powerful handle for controlling nanofiber structure, avidity, and function, we present a robust, translatable platform for advancing targeted imaging and therapy in CD38-positive malignancies. PubMed: 42011845DOI: 10.1021/acsabm.6c00348 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.41 Å) |
Structure validation
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