The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Bond-centric modular design of protein assemblies
Open accessPreprint — published as 10.1038/s41563-025-02297-5 · Paper page
Abstract
We describe a modular bond-centric approach to protein nanomaterial design inspired by the rich diversity of chemical structures that can be generated from the small number of atomic valencies and bonding interactions. We design protein building blocks with regular coordination geometries and bonding interactions that enable the assembly of a wide variety of closed and opened nanomaterials using simple geometrical principles. Experimental characterization confirms successful formation of more than twenty multi-component polyhedral protein cages, 2D arrays, and 3D protein lattices, with a high (10-50 %) success rate and electron microscopy data closely matching the corresponding design models. Because of the modularity, individual building blocks can assemble with different partners to generate distinct regular assemblies, resulting in an economy of parts and enabling the construction of reconfigurable systems.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Flagged first, then by citations
Metadata
- Authors
- Wang, S., Favor, A., Kibler, R. D., Lubner, J. M., Borst, A. J., Coudray, N., Redler, R., Chiang, H. T., Sheffler, W., Hsia, Y., Li, Z., Ekiert, D. C., Bhabha, G., Pozzo, L. D., & Baker, D.
- Affiliations
- University of Washington (US)
- Johns Hopkins University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Wang, Shunzhi
- Baker, David
- ORCID
- Venue
- Nature Materials
- Publisher
- openRxiv
- Published
- 2024-10-12
- Volume
- 24
- Issue
- 10
- Pages
- 1644-1652
- ISSN
- 1476-1122 (ISSN-L)
- PMC
- PMC12484077
- OpenAlex
- W4412780842
- Cited by
- 22
- References
- 1
- Citations by year
- 2026: 16 · 2025: 6
- FWCI
- 4.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature Materials (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed Central (submittedVersion, cc-by)
- Funders
- National Science Foundation (HDTRA1-19-1-0003, 2308979, 2116265)
- Howard Hughes Medical Institute
- U.S. Department of Energy (DESC0019288)
- U.S. Department of Health and Human Services (R01AG063845, U24 GM129539, R35GM128777)
- Burroughs Wellcome Fund (1199630)
- Bill and Melinda Gates Foundation (OPP1156262)
- Washington Research Foundation
- Amgen
- National Institutes of Health (SF349247, SCR_019202, OPP1156262)
- School of Medicine, New York University
- National Institute on Aging (R01AG063845)
- National Institute of General Medical Sciences (U24GM129539, R35GM128777)
- Division of Materials Research (DMR-2116265, DMR-2308979, 2116265, 2308979)
- Common Fund (U24 GM129539)
- Energy Frontier Research Centers (DE-SC0019288)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- protein self-assembly, protein nanomaterials, modular protein design, coordination geometry, protein microarrays, directional interactions
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
