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10SD

The cryoEM structure of T10 type2 nanofiber

Summary for 10SD
Entry DOI10.2210/pdb10sd/pdb
EMDB information75431
DescriptorT10 type 2 nanofiber, DECANOIC ACID (2 entities in total)
Functional Keywordsnanofiber, protein fibril
Biological sourcesynthetic construct
More
Total number of polymer chains16
Total formula weight19880.50
Authors
Zhang, H.,Yang, Y. (deposition date: 2026-02-05, release date: 2026-06-17)
Primary citationGodbe, 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: 42011845
DOI: 10.1021/acsabm.6c00348
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.11 Å)
Structure validation

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