Evidence map›Paper›PMID 41816938›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

Design of Optical Transducer for Recognition of Biomolecular Interactions between Bacterial Lipopolysaccharides and Amino Acids.

Yena Choi, Sangmin Lee, Jin-Kang Choi, Hyunsoo Han, Yeongseon Choi, Jun-Hyung Im, Hyein Kim, Sangmin Jeon, Minjae Lee, Chang Yun Son and 1 more

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 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

11 authors.

Yena ChoiDepartment of Chemical Engineering, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Sangmin LeeDepartment of Chemistry, Seoul National University, Seoul, Republic of Korea.
Jin-Kang ChoiDepartment of Chemical Engineering, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Hyunsoo HanDepartment of Chemical Engineering, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Yeongseon ChoiDepartment of Chemical Engineering, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Jun-Hyung ImDepartment of Chemical Engineering, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Hyein KimDepartment of Chemical Engineering, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Sangmin JeonDepartment of Chemical Engineering, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.ORCID https://orcid.org/0000-0002-5489-2150
Minjae LeeDepartment of Energy Science & Engineering, Department of Chemistry, Kunsan National University, Gunsan, Republic of Korea.
Chang Yun SonDepartment of Chemistry, Seoul National University, Seoul, Republic of Korea.ORCID https://orcid.org/0000-0002-0784-6565
Young-Ki KimDepartment of Chemical Engineering, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.ORCID https://orcid.org/0000-0002-4420-3489

Funding

National Research Foundation of Korea 2022M3C1A3081312National Research Foundation of Korea RS-2023-00212739National Research Foundation of Korea RS-2023-00302586National Research Foundation of Korea RS-2024-00411809
6 · The paper itself

Abstract

Recognition of biomolecular phenomena at interfaces is a key scientific challenge with fundamental and practical importance. In this work, we discover two structurally similar amino acids, glutamic acid (Glu) and aspartic acid (Asp), showing different biological functions, have a significant but distinct orientational coupling with liquid crystals (LCs). Combining experiments with density functional theory calculations, we reveal that Glu and Asp exhibit unique adsorption-desorption dynamics at the LC-aqueous interfaces, producing distinct macroscopic optical signals. These interfacial behaviors are specifically governed by pH condition of the aqueous solution because the pH variations cause significant changes in charge states of the amino acids and thus their intermolecular interactions with LCs. Additionally, the dynamics are also modulated by the presence of other biological molecules (e.g., bacterial byproducts of Salmonella lipopolysaccharide, Staphylococcus aureus lipoteichoic acid, and Escherichia coli lipopolysaccharide) forming complexes with the amino acids, which dramatically change the LC's optical response. Leveraging this specific recognition mechanism for the interfacial dynamics of biomolecules and their interactions with other biological species, we also demonstrate the practical LC systems that autonomously recognize and optically report Salmonella at trace concentrations (10

Indexed as

Amino AcidsAspartic AcidGlutamic AcidLipopolysaccharidesLiquid CrystalsEscherichia coliHydrogen-Ion ConcentrationSalmonellaStaphylococcus aureusAmino AcidsAspartic AcidGlutamic AcidLipopolysaccharidesamino acidsaspartic acidsbiomolecular interactionsglutamic acidsliquid crystalssalmonella

Identifiers

PMID41816938
PMCPMC13205851

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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.