Evidence map›Paper›PMID 38724718›Full record

ArticleNature structural & molecular biology2024

Computational design of non-porous pH-responsive antibody nanoparticles.

Erin C Yang, Robby Divine, Marcos C Miranda, Andrew J Borst, Will Sheffler, Jason Z Zhang, Justin Decarreau, Amijai Saragovi, Mohamad Abedi, Nicolas Goldbach and 15 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. From sequence to scaffold: Computational design of protein nanoparticle vaccines from AlphaFold2-predicted building blocks.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Antibody-Nanoparticle Conjugates in Therapy: Combining the Best of Two Worlds.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Review
  14. Article
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

25 authors.

Erin C YangInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0002-1305-9066
Robby DivineInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Marcos C MirandaInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0002-2839-6997
Andrew J BorstInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0003-4297-7824
Will ShefflerInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Jason Z ZhangInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0003-0091-6273
Justin DecarreauInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Amijai SaragoviInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Mohamad AbediInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Nicolas GoldbachInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0001-5401-3892
Maggie AhlrichsInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0002-4793-3890
Craig DobbinsInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Alexis HandInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Suna ChengInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Mila LambInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Paul M LevineInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Sidney ChanInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0002-1617-0464
Rebecca SkotheimInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Jorge FallasInstitute for Protein Design, University of Washington, Seattle, WA, USA.
George UedaInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0002-9792-7149
Joshua LubnerInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0003-1506-0949
Masaharu SomiyaInstitute for Protein Design, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0002-5607-8128
Alena KhmelinskaiaInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Neil P KingInstitute for Protein Design, University of Washington, Seattle, WA, USA. neilking@uw.edu.ORCID http://orcid.org/0000-0002-2978-4692
David BakerInstitute for Protein Design, University of Washington, Seattle, WA, USA. dabaker@uw.edu.ORCID http://orcid.org/0000-0001-7896-6217

Funding

Structure-based design of broadly protective coronavirus vaccinesP01AI167966 · NIAID · UNIVERSITY OF WASHINGTON · PI BALI PULENDRAN · 2022 to 2026
$15.3M
Designed Vehicles for Blood Brain Barrier TraversalR01AG063845 · NIA · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2019 to 2023
$2.5M
High resolution structure modeling with RosettaR01GM092802 · NIGMS · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2010 to 2017
$2.3M
Design of de novo interleukin mimics for targeted immunotherapyR01CA240339 · NCI · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2019 to 2023
$2.1M
Synthetic nucleocapsids: a new peptide library platformR21CA232430 · NCI · UNIVERSITY OF WASHINGTON · PI KING, NEIL, PUN, SUZIE H. · 2018 to 2019
$366k
Howard Hughes Medical InstituteNCI NIH HHS R01 CA240339NCI NIH HHS R21 CA232430NIAID NIH HHS P01 AI167966NIA NIH HHS R01 AG063845NIGMS NIH HHS R01 GM092802
6 · The paper itself

Abstract

Programming protein nanomaterials to respond to changes in environmental conditions is a current challenge for protein design and is important for targeted delivery of biologics. Here we describe the design of octahedral non-porous nanoparticles with a targeting antibody on the two-fold symmetry axis, a designed trimer programmed to disassemble below a tunable pH transition point on the three-fold axis, and a designed tetramer on the four-fold symmetry axis. Designed non-covalent interfaces guide cooperative nanoparticle assembly from independently purified components, and a cryo-EM density map closely matches the computational design model. The designed nanoparticles can package protein and nucleic acid payloads, are endocytosed following antibody-mediated targeting of cell surface receptors, and undergo tunable pH-dependent disassembly at pH values ranging between 5.9 and 6.7. The ability to incorporate almost any antibody into a non-porous pH-dependent nanoparticle opens up new routes to antibody-directed targeted delivery.

Indexed as

NanoparticlesAntibodiesCryoelectron MicroscopyHumansHydrogen-Ion ConcentrationModels, MolecularPorosityAntibodies

Identifiers

PMID38724718
PMCPMC11402598

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.