Evidence map›Paper›PMID 42766017›Full record

ArticleArchives of microbiology2026

Deep learning-driven de novo discovery of binders targeting the transmembrane domain of BamA.

Minghui Du, Yuqiao Xin, Benao Xu, Yang Zhang, Linjie Han, Bingjie Ji, Jian Zhao, Yongshan Zhao

Abstract read
PubMed Publisher
In one paragraph

Article in Archives of microbiology, 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.

Minghui DuSchool of Life Science and Bio-Pharmaceutics, Shenyang Pharmaceutical University, 103 Wenhua Road, Shenhe District, Shenyang, 110016, Liaoning, China.
Yuqiao XinSchool of Life Science and Bio-Pharmaceutics, Shenyang Pharmaceutical University, 103 Wenhua Road, Shenhe District, Shenyang, 110016, Liaoning, China.
Benao XuSchool of Life Science and Bio-Pharmaceutics, Shenyang Pharmaceutical University, 103 Wenhua Road, Shenhe District, Shenyang, 110016, Liaoning, China.
Yang ZhangSchool of Life Science and Bio-Pharmaceutics, Shenyang Pharmaceutical University, 103 Wenhua Road, Shenhe District, Shenyang, 110016, Liaoning, China.
Linjie HanSchool of Life Science and Bio-Pharmaceutics, Shenyang Pharmaceutical University, 103 Wenhua Road, Shenhe District, Shenyang, 110016, Liaoning, China.
Bingjie JiSchool of Life Science and Bio-Pharmaceutics, Shenyang Pharmaceutical University, 103 Wenhua Road, Shenhe District, Shenyang, 110016, Liaoning, China.
Jian ZhaoDepartment of Pharmacology, Shenyang Pharmaceutical University, Shenyang, 110016, China.
Yongshan ZhaoSchool of Life Science and Bio-Pharmaceutics, Shenyang Pharmaceutical University, 103 Wenhua Road, Shenhe District, Shenyang, 110016, Liaoning, China. zhao_syphu@163.com.

Funding

Natural Science Foundation of Liaoning Province No. 2024-MS-089
6 · The paper itself

Abstract

Antimicrobial resistance (AMR) is an escalating global health threat, with multidrug-resistant Gram-negative bacteria presenting a particularly serious clinical challenge. The unique outer membrane (OM) structure serves as a natural barrier against conventional therapeutics, so that treatment strategies become more complicated. Notably, drug development aimed at the transmembrane (TM) domains of membrane proteins remains highly limited. To overcome this bottleneck, we established an artificial intelligence (AI)-driven framework for the design and screening of BamA transmembrane (TM) domain-targeting binders. This framework employs a multi-channel convolutional neural network (DeepTM-Bind), which integrates heterogeneous protein features to achieve high predictive accuracy. Building upon this foundation, we further developed a multidimensional evaluation system to guide de novo design strategies. Using this integrated approach, binders targeting the lateral gate of BamA were successfully generated. All-atom molecular dynamics (MD) simulations within a membrane environment, combined with multiscale mechanistic analyses, confirmed the structural stability and strong binding potential of the candidate molecules, and revealed a previously unrecognized binding mode. Collectively, this study introduces an advanced computational paradigm for therapeutic design targeting TM domains and provides a promising strategy to combat multidrug-resistant Gram-negative pathogens.

Indexed as

Anti-Bacterial AgentsBacterial Outer Membrane ProteinsDeep LearningEscherichia coli ProteinsDrug DesignDrug DiscoveryEscherichia coliMolecular Dynamics SimulationProtein BindingProtein DomainsAnti-Bacterial AgentsBacterial Outer Membrane ProteinsBamA protein, E coliEscherichia coli ProteinsDeep learningDe novo designMultisource featureTransmembrane protein

Identifiers

What OpenQuestion holds

Textmetadata
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.