Evidence map›Paper›PMID 37293959›Full record

ArticleNucleic acids research2023

An amber-encoding helper phage for more efficient phage display of noncanonical amino acids.

Joshua Trae Hampton, Chia-Chuan Dean Cho, Demonta D Coleman, Zhi Zachary Geng, Peng-Hsun Chase Chen, Gopal K Dubey, Lauralee D Sylvain, Shiqing Xu, Wenshe Ray Liu

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
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

11 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Expanding the Genetic Code with Lysine Aminoacylation.Journal of the American Chemical Society · 2026
    Article
  4. Incorporation of Butyryl-Lysine into Phage-Displayed Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Pharmacophore-driven antibody discovery on the yeast surface.bioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Review
  8. Article
  9. Review
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  11. Review
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

9 authors at 1 institution in 1 country.

Joshua Trae HamptonTexas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Chia-Chuan Dean ChoTexas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Demonta D ColemanTexas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Zhi Zachary GengTexas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Peng-Hsun Chase ChenTexas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Gopal K DubeyTexas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Lauralee D SylvainTexas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Shiqing XuTexas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Wenshe Ray LiuTexas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.ORCID 0000-0002-7078-6534
Texas A&M University · US

Funding

Use of the Noncanonical Amino Acid Mutagenesis Technique in Combination with Other Approaches to Study Functions of Posttranslational Lysine Modifications in ProteinsR35GM145351 · NIGMS · TEXAS A&M UNIVERSITY · PI Wenshe Ray Liu · 2022 to 2026
$2.6M
NIGMS NIH HHS R35 GM145351
6 · The paper itself

Abstract

Using an amber suppression-based noncanonical amino acid (ncAA) mutagenesis approach, the chemical space in phage display can be significantly expanded for drug discovery. In this work, we demonstrate the development of a novel helper phage, CMa13ile40, for continuous enrichment of amber obligate phage clones and efficient production of ncAA-containing phages. CMa13ile40 was constructed by insertion of a Candidatus Methanomethylophilus alvus pyrrolysyl-tRNA synthetase/PylT gene cassette into a helper phage genome. The novel helper phage allowed for a continuous amber codon enrichment strategy for two different libraries and demonstrated a 100-fold increase in packaging selectivity. CMa13ile40 was then used to create two peptide libraries containing separate ncAAs, Nϵ-tert-butoxycarbonyl-lysine and Nϵ-allyloxycarbonyl-lysine, respectively. These libraries were used to identify peptide ligands that bind to the extracellular domain of ZNRF3. Each selection showed differential enrichment of unique sequences dependent upon the ncAA used. Peptides from both selections were confirmed to have low micromolar affinity for ZNRF3 that was dependent upon the presence of the ncAA used for selection. Our results demonstrate that ncAAs in phages provide unique interactions for identification of unique peptides. As an effective tool for phage display, we believe that CMa13ile40 can be broadly applied to a wide variety of applications.

Indexed as

Amino AcidsAmino Acyl-tRNA SynthetasesBacteriophagesCell Surface Display TechniquesDrug DiscoveryPeptidesAmino AcidsAmino Acyl-tRNA SynthetasesPeptides

Identifiers

PMID37293959
PMCPMC10359598
OpenAlexW4379967462

What OpenQuestion holds

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LicenceCC BY-NC
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.