Evidence map›Paper›PMID 42657195›Full record

ArticleJACS Au2026

Enhancing Enzyme Activity Via Noncovalent Association with DNA-Functionalized Nanoparticles.

Seungheon Lee, Atri Bhattacharya, Regan Kuttler, Subrata Pandit, Busra Ozguney, Jackson Jacobi, Jeetain Mittal, Devleena Samanta

Abstract read
In one paragraph

Article in JACS Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Seungheon LeeDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID https://orcid.org/0000-0001-9631-4853
Atri BhattacharyaDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
Regan KuttlerArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, Texas 77843, United States.
Subrata PanditDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID https://orcid.org/0009-0000-3968-716X
Busra OzguneyArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, Texas 77843, United States.ORCID https://orcid.org/0000-0003-2025-0149
Jackson JacobiDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
Jeetain MittalArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, Texas 77843, United States.ORCID https://orcid.org/0000-0002-9725-6402
Devleena SamantaDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID https://orcid.org/0000-0002-0647-7673

Funding

Multiscale Computational Models to Investigate the Role of Phase Separation in BiologyR35GM153388 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI Jeetain Mittal · 2024 to 2026
$1.3M
NIGMS NIH HHS R35 GM153388
6 · The paper itself

Abstract

Enhancing enzyme performance without protein engineering remains a central challenge in biocatalysis. Here, we report the unusual discovery that nanoparticles densely functionalized with DNA, commonly known as spherical nucleic acids (SNAs), can bind enzymes without chemical conjugation, affinity tags, or engineered recognition motifs and substantially increase catalytic activity. Using cytochrome c as a model peroxidase, we show that noncovalent binding to SNAs increases the apparent turnover number by up to 15-fold. Mechanistic studies by varying DNA density, length, and nanoparticle core identity reveal that activity enhancement does not arise from free DNA or the nanoparticle core alone but from the three-dimensional, high-density presentation of DNA at the nanoparticle surface. Consequently, similar effects are observed when gold cores are replaced with glucose oxidase or antibody cores. Moreover, activity modulation also depends on DNA sequence, establishing sequence design as a programmable handle for tuning enzyme output. All-atom molecular dynamics simulations, binding studies, and circular dichroism further reveal that base-specific interactions reshape enzyme conformational flexibility and increase active-site accessibility. This effect generalizes beyond cytochrome c to catalase and carbonic anhydrase. Together, these findings establish SNAs as adaptable, sequence-programmable platforms for enhancing and coordinating biocatalysis and expand their functional scope into enzyme regulation.

Indexed as

DNAEnzymatic activityligandnoncovalentspherical nucleic acids

Identifiers

PMID42657195
PMCPMC13508087

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.