Evidence map›Paper›PMID 40159649›Full record

ArticleACS applied materials & interfaces2025

Modular Platform for Efficient Assembly of Multifunctional Antibodies Using Orthogonal Protein-Protein Interactions.

Baizhen Gao, Rushant Sabnis, Siddhi Kotnis, Sofia Feliciano, Kyge Poling, Tracy Mei, Min Feng, Jugal Kishore Das, Jianxun Song, Qing Sun

Abstract read
In one paragraph

Article in ACS applied materials & interfaces, 2025. 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

10 authors.

Baizhen GaoDepartment of Chemical Engineering, Texas A&M University, College Station, Texas 77840, United States.ORCID 0009-0006-6159-8247
Rushant SabnisDepartment of Chemical Engineering, Texas A&M University, College Station, Texas 77840, United States.
Siddhi KotnisDepartment of Chemical Engineering, Texas A&M University, College Station, Texas 77840, United States.ORCID 0009-0006-7144-2748
Sofia FelicianoDepartment of Chemical Engineering, Texas A&M University, College Station, Texas 77840, United States.
Kyge PolingDepartment of Chemical Engineering, Texas A&M University, College Station, Texas 77840, United States.
Tracy MeiDepartment of Chemical Engineering, Texas A&M University, College Station, Texas 77840, United States.
Min FengDepartment of Chemical Engineering, Texas A&M University, College Station, Texas 77840, United States.
Jugal Kishore DasDepartment of Microbial Pathogenesis and Immunology, Texas A&M University Health Science Center, Bryan, Texas 77807, United States.ORCID 0000-0002-4553-2196
Jianxun SongDepartment of Microbial Pathogenesis and Immunology, Texas A&M University Health Science Center, Bryan, Texas 77807, United States.
Qing SunDepartment of Chemical Engineering, Texas A&M University, College Station, Texas 77840, United States.

Funding

Combating melanoma with an attenuated bacterial therapeuticR01CA273002 · NCI · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI Jianxun Jim Song · 2023 to 2026
$1.8M
A deep learning and experiment integrated platform for stable mRNA vaccines developmentR01AI165433 · NIAID · TEXAS ENGINEERING EXPERIMENT STATION · PI qing sun · 2022 to 2026
$1.8M
NCI NIH HHS R01 CA273002NIAID NIH HHS R01 AI165433
6 · The paper itself

Abstract

Multifunctional antibodies, capable of simultaneously engaging multiple targets, are a unique class of antibodies that have sparked growing interest. Current approaches for making multifunctional antibodies, including chemical conjugation or genetic modifications, suffer from low product yield, complex structure design, and complicated manufacturing processes. In this study, we report a modular post-translational platform with highly specific protein-protein interactions for multifunctional antibody assembly and an elastin-like polypeptide (ELP) for easy purification. We generated and purified multifunctional antibodies with over 90% assembled scaffold and overall product purity. Additionally, we assembled antibodies with diverse applications, including detecting cancer, inhibiting cancer cell growth, and directing T cells to cancer cells for enhanced therapeutic efficacy. This platform offers high assembly efficiency, easy purification, and modularity for the redesign of antibody functions.

Indexed as

AntibodiesAnimalsCell Line, TumorElastinHumansPeptidesAntibodiesElastinPeptidesantibody engineeringelastin-like polypeptide (ELP)nanobodyprotein−protein interactionprotein purification

Identifiers

PMID40159649
PMCPMC11986891

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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.