Evidence map›Paper›PMID 41455806›Full record

ArticleScientific reports2025

LLPS droplet size estimation via UV-Vis spectroscopy using a microplate reader.

Mayu Enomoto-Kusano, Takashi S Kodama, Suai Anzawa, Kyoko Furuita, Ryoga Kobayashi, Naotaka Sekiyama, Wataru Togawa, Toshimichi Fujiwara, Yohei Miyanoiri, Hidehito Tochio and 1 more

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
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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.

Mayu Enomoto-Kusano *Graduate School of Engineering Science, Yokohama National University, Tokiwadai 79-5, Hodogaya-ku, Yokohama, 240-8501, Japan.
Takashi S Kodama *Institute for Protein Research, The University of Osaka, Yamadaoka 3-2, Suita, 565-0871, Osaka, Japan. tskodama@protein.osaka-u.ac.jp.
Suai AnzawaGraduate School of Engineering Science, Yokohama National University, Tokiwadai 79-5, Hodogaya-ku, Yokohama, 240-8501, Japan.
Kyoko FuruitaInstitute for Protein Research, The University of Osaka, Yamadaoka 3-2, Suita, 565-0871, Osaka, Japan.
Ryoga KobayashiDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, 606-8502, Japan.
Naotaka SekiyamaDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, 606-8502, Japan.
Wataru TogawaGraduate School of Engineering Science, Yokohama National University, Tokiwadai 79-5, Hodogaya-ku, Yokohama, 240-8501, Japan.
Toshimichi FujiwaraInstitute for Protein Research, The University of Osaka, Yamadaoka 3-2, Suita, 565-0871, Osaka, Japan.
Yohei MiyanoiriInstitute for Protein Research, The University of Osaka, Yamadaoka 3-2, Suita, 565-0871, Osaka, Japan.
Hidehito TochioDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, 606-8502, Japan.
Chojiro KojimaGraduate School of Engineering Science, Yokohama National University, Tokiwadai 79-5, Hodogaya-ku, Yokohama, 240-8501, Japan. kojima-chojiro-xk@ynu.ac.jp.

Funding

Agency for Cultural Affairs, Government of Japan NMR PlatformInstitute for Protein Research, Osaka University CR-24-05Japan Agency for Medical Research and Development JP24ama121001Japan Science and Technology Agency JPMJSP2178Japan Society for the Promotion of Science JP22H05536, JP22K19184, JP23K27109, and JP23K18030Japan Society for the Promotion of Science JP25KJ0230Ministry of Education, Culture, Sports, Science and Technology NMR Platform
6 · The paper itself

Abstract

Liquid-liquid phase separation (LLPS) is critical to the formation of membraneless organelles within cells. Monitoring the size and dynamics of LLPS droplets is essential to understanding their function. However, conventional methods, such as microscopy and dynamic light scattering (DLS), have limitations, including low throughput and complex setups. Here, we present a simple, label-free, high-throughput method for estimating droplet size using ultraviolet-visible (UV-Vis) spectra obtained using a standard microplate reader. This method is theoretically supported by Mie scattering theory. By analyzing the spectral shape and comparing it to that of glass beads of known sizes, our method enables the quantitative estimation of LLPS droplet size in a minimally invasive manner. We validated our approach using peptide droplets of known sizes, then applied it to monitor the growth of protein condensates formed by vesicle-associated membrane protein-associated protein B (VAPB). This technique offers a convenient, scalable alternative for screening LLPS dynamics in various biomolecular systems.

Indexed as

Spectrophotometry, UltravioletParticle Size

Identifiers

PMID41455806
PMCPMC12847920

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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.