Evidence map›Paper›PMID 41479173›Full record

ArticleAngewandte Chemie (International ed. in English)2026

An Expanded Toolbox for Versatile Chemical Editing of Adeno-Associated Virus.

Quan Pham, Jake Glicksman, Boyang Han, David Koo, Conor Loynd, Soumya Jyoti Singha Roy, Abhishek Chatterjee

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. An Expanded Toolbox for Versatile Chemical Editing of Adeno-Associated Virus.Angewandte Chemie (International ed. in English) · 2026
    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

7 authors.

Quan PhamDepartment of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, Massachusetts, 02467, USA.ORCID 0009-0001-9559-7772
Jake GlicksmanDepartment of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, Massachusetts, 02467, USA.
Boyang HanDepartment of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, Massachusetts, 02467, USA.
David KooDepartment of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, Massachusetts, 02467, USA.
Conor LoyndDepartment of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, Massachusetts, 02467, USA.
Soumya Jyoti Singha RoyDepartment of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, Massachusetts, 02467, USA.ORCID 0000-0002-7999-4591
Abhishek ChatterjeeDepartment of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, Massachusetts, 02467, USA.ORCID 0000-0002-6231-5302

Funding

The GCE4All Center: Unleashing the Potential of Genetic Code Expansion for Biomedical ResearchRM1GM144227 · NIGMS · OREGON STATE UNIVERSITY · PI RYAN A MEHL · 2022 to 2026
$6.2M
A genetically encoded toolset to decipher the biology of post-translational modifications in the mammalian proteomeR35GM136437 · NIGMS · BOSTON COLLEGE · PI Abhishek Chatterjee · 2020 to 2026
$4.0M
National Science Foundation 2128185NIGMS NIH HHS R35 GM136437NIGMS NIH HHS RM1 GM144227NIGMS NIH HHS RM1-GM144227NIH HHS R35GM136437
6 · The paper itself

Abstract

Site-specific incorporation of noncanonical amino acids (ncAAs) into the adeno-associated virus (AAV) capsid offers powerful opportunities to probe and engineer the properties of this leading vector for human gene therapy. However, this approach currently relies almost exclusively on a single azide-containing ncAA, incorporated using the pyrrolysyl-tRNA synthetase/tRNA pair. Here, we substantially broaden the scope of this technology by demonstrating successful incorporation of numerous ncAAs into AAV capsid using four different platforms, and by uncovering design principles that facilitate capsid tolerance to structurally diverse side chains. Using this expanded toolbox, we incorporate several different bioorthogonal conjugation handles into AAV for precise capsid modification. In particular, a tetrazine-containing ncAA facilitated ultrafast conjugation of an anti-HER2 nanobody to the capsid, creating conjugates that efficiently and selectively infect HER2+ cells. We further used this platform for optimized capsid PEGylation, which reduced its immunogenicity without compromising infectivity. Finally, we efficiently incorporated two distinct ncAAs into the AAV capsid, and subsequently labeled them orthogonally to attach two different entities. Together, these advances dramatically expand the chemistries that can be introduced into the AAV capsid, offering powerful new tools to both probe and engineer the properties of this promising gene therapy vector.

Indexed as

Amino AcidsDependovirusCapsidCapsid ProteinsHumansAmino AcidsCapsid ProteinsAAV engineeringBioorthogonal chemistryGene therapyGenetic code expansionNoncanonical amino acids

Identifiers

PMID41479173
PMCPMC12887607

What OpenQuestion holds

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LicenceCC BY
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.