Evidence map›Paper›PMID 41243883›Full record

ArticleAngewandte Chemie (International ed. in English)2026

Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.

Darwin C Gomez, Swarnadeep Seth, Ronnie Mondal, Stephen J Koehler, Jared G Baker, Charles Plate, Ian C Anderson, Mikayla R Smith, Joey Gloriod, Morgan Gunter and 3 more

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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.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

13 authors.

Darwin C GomezMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Swarnadeep SethDepartment of Chemical Engineering, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Ronnie MondalMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Stephen J KoehlerMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Jared G BakerMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Charles PlateDepartment of Chemical Engineering, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Ian C AndersonMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Mikayla R SmithMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Joey GloriodMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Morgan GunterMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Valerie V WelbornMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.
Sanket A DeshmukhDepartment of Chemical Engineering, Virginia Tech, Blacksburg, Virginia, 24061, USA.
C Adrian FiggMacromolecules Innovation Institute and Department of Chemistry, Virginia Tech, Blacksburg, Virginia, 24061, USA.ORCID 0000-0003-3514-7750

Funding

Elucidating the dynamical and structural molecular factors at the origin of non-enzymatic protein-protein and protein-DNA cross-linksR35GM150409 · NIGMS · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI Valerie Vaissier Welborn · 2023 to 2026
$1.5M
National Science Foundation DMR-1933525NIGMS NIH HHS R35 GM150409NIGMS NIH HHS R35-GM150409
6 · The paper itself

Abstract

Molecular definition is usually regarded as a prerequisite to achieve protein recognition and functional modulation, particularly for macromolecular interactions. Herein, we report that polymers with specific combinations of monomers arranged into random sequences [random hetero oligomers (RHOs)] can selectively bind to a model protein. Using green fluorescent protein (GFP) as a target, polyacrylates were developed that bound with nanomolar affinity and enhanced fluorescence by >100%. Purification of the polymerization product revealed subpopulations of compositions with distinct affinities and selectivity for GFP over a competing protein. Experimental and computational binding analyses confirmed that there are distinct RHO-GFP interactions, which are influenced by RHO chemical composition. These findings show that sequence-defined structures are not a prerequisite for selective protein recognition. Synthetic polymers can instead serve as scalable, tunable platforms for molecular recognition-representing a significant leap towards next-generation sensing, therapeutic, responsive, and catalytic materials in domains previously dominated by biologics or complex peptide scaffolds.

Indexed as

Acrylic ResinsGreen Fluorescent ProteinsAcrylic Resinscarbopol 940Green Fluorescent ProteinsCopolymersPolymer–protein conjugatePolymer synthesisProteinRAFT

Identifiers

PMID41243883
PMCPMC12790347

What Socratic holds

Textmetadata
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 Socratic graph.