Evidence map›Paper›PMID 41756926›Full record

ArticlebioRxiv : the preprint server for biology2026

Intracellular Delivery of Peptides and Proteins with an Engineered Membrane Translocation Domain.

Prabhat Bhat, Heba Salim, Jeremy L Ritchey, Na Li, Brendan B Harty, Thomas Patel, Jing Zhao, Qi-En Wang, Virginia L King, Louis Tartaglia and 2 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

5 · Who and what money

Authors and funding

12 authors.

Prabhat BhatDepartment of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.ORCID 0000-0001-6421-9341
Heba SalimDepartment of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.ORCID 0009-0007-9352-6819
Jeremy L RitcheyDepartment of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.
Na LiDepartment of Radiation Oncology, The Ohio State University, Columbus, Ohio 43210, United States.
Brendan B HartyDepartment of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.ORCID 0000-0003-2811-9284
Thomas PatelDepartment of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.
Jing ZhaoDepartment of Physiology and Cell Biology, Dorothy M. Davis Heart and Lung Research Institute, College of Medicine, The Ohio State University, Columbus, Ohio 43210, United States.
Qi-En WangDepartment of Radiation Oncology, The Ohio State University, Columbus, Ohio 43210, United States.ORCID 0000-0002-3759-2148
Virginia L KingPermeasis Therapeutics, 349 Newbury Street, Boston, Massachusetts 02115, United States.ORCID 0000-0002-9493-5426
Louis TartagliaPermeasis Therapeutics, 349 Newbury Street, Boston, Massachusetts 02115, United States.
Jenő GyurisPermeasis Therapeutics, 349 Newbury Street, Boston, Massachusetts 02115, United States.
Dehua PeiDepartment of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, United States.ORCID 0000-0002-2057-6934

Funding

Translational Therapeutics Research Program (TT)P30CA016058 · NCI · OHIO STATE UNIVERSITY · PI Daniel G. Stover · 1985 to 2026
$132.3M
Development of Cell-Permeable Peptides and ProteinsR35GM122459 · NIGMS · OHIO STATE UNIVERSITY · PI Dehua Pei · 2017 to 2026
$5.1M
NCI NIH HHS P30 CA016058NIGMS NIH HHS R35 GM122459
6 · The paper itself

Abstract

Antibodies and other protein therapeutics have revolutionized medicine, but their application is largely limited to extracellular targets. The lack of efficient intracellular delivery methods remains a major bottleneck. Here, we engineered a family of small (~90 amino acids), metabolically stable membrane translocation domains (MTDs) by modifying the loop sequences of a human fibronectin type III (FN3) domain. The most potent variant, MTD4, is highly cell-permeable and can be recombinantly fused to the N- or C-terminus of any peptide or protein, serving as a versatile "plug-and-play" vehicle. We demonstrate that MTD4 fusions efficiently deliver a wide variety of functional peptides and proteins into the cytosol and nucleus of eukaryotic cells, both

Identifiers

PMID41756926
PMCPMC12934630

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.