Evidence map›Paper›PMID 37040364›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2023

Empty and Full AAV Capsid Charge and Hydrophobicity Differences Measured with Single-Particle AFM.

Caryn L Heldt, Oluwatoyin Areo, Pratik U Joshi, Xue Mi, Yulia Ivanova, Alex Berrill

Abstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Physical Changes of Biomacromolecules upon Covalent Surface Immobilization.Langmuir : the ACS journal of surfaces and colloids · 2026
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. The amazing AAV capsids: Into the structure-verse.Molecular therapy. Methods & clinical development · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Caryn L HeldtDepartment of Chemical Engineering, Michigan Technological University, Houghton, Michigan 49931, United States.ORCID 0000-0002-0776-8763
Oluwatoyin AreoDepartment of Chemical Engineering, Michigan Technological University, Houghton, Michigan 49931, United States.
Pratik U JoshiDepartment of Chemical Engineering, Michigan Technological University, Houghton, Michigan 49931, United States.ORCID 0000-0002-8257-5830
Xue MiDepartment of Chemical Engineering, Michigan Technological University, Houghton, Michigan 49931, United States.ORCID 0000-0002-8771-1547
Yulia IvanovaGene Therapy Process Development, Bioprocess Research and Development, Biotherapeutics Pharmaceutical Sciences, Pfizer, Chesterfield, Missouri 63017, United States.
Alex BerrillGene Therapy Process Development, Bioprocess Research and Development, Biotherapeutics Pharmaceutical Sciences, Pfizer, Chesterfield, Missouri 63017, United States.

Funding

Dense Phase Polyelectrolytes to Thermally Stabilize Viral VaccinesR21AI150962 · NIAID · MICHIGAN TECHNOLOGICAL UNIVERSITY · PI HELDT, CARYN, PERRY, SARAH LOUISE · 2020 to 2021
$429k
NIAID NIH HHS R21 AI150962
6 · The paper itself

Abstract

Adeno-associated virus (AAV) is showing promise as a therapy for diseases that contain a single-gene deletion or mutation. One major scale-up challenge is the removal of empty or non-gene of interest containing AAV capsids. Analytically, the empty capsids can be separated from full capsids using anion exchange chromatography. However, when scaled up to manufacturing, the minute changes in conductivity are difficult to consistently obtain. To better understand the differences in the empty and full AAV capsids, we have developed a single-particle atomic force microscopy (AFM) method to measure the differences in the charge and hydrophobicity of AAV capsids at the single-particle level. The atomic force microscope tip was functionalized with either a charged or a hydrophobic molecule, and the adhesion force between the functionalized atomic force microscope tip and the virus was measured. We measured a change in the charge and hydrophobicity between empty and full AAV2 and AAV8 capsids. The charge and hydrophobicity differences between AAV2 and AAV8 are related to the distribution of charge on the surface and not the total charge. We propose that the presence of nucleic acids inside the capsid causes minor but measurable changes in the capsid structure that lead to measurable surface changes in charge and hydrophobicity.

Indexed as

CapsidDependovirusCapsid ProteinsGenetic VectorsMicroscopy, Atomic ForceCapsid Proteins

Identifiers

PMID37040364
PMCPMC10135413

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.