Evidence map›Paper›PMID 40784560›Full record

ArticleSLAS discovery : advancing life sciences R & D2025

Aurora 2.0: A fluorogenic dye library for expanding the capability of protein-adaptive differential scanning fluorimetry (paDSF).

Annemarie F Charvat, Kayleigh Mason-Chalmers, Aneta Grabinska-Rogala, Shloka Shivakumar, Zachary Gale-Day, Taiasean Wu, Zoe Millbern, Jonathan B Grimm, Emma C Carroll, K Peter R Nilsson and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in SLAS discovery : advancing life sciences R & D, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

13 authors.

Annemarie F CharvatInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, CA 94158, USA; Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, USA.
Kayleigh Mason-ChalmersInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, CA 94158, USA.
Aneta Grabinska-RogalaInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, CA 94158, USA.
Shloka ShivakumarInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, CA 94158, USA.
Zachary Gale-DayInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, CA 94158, USA; Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, USA.
Taiasean WuInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, CA 94158, USA; Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, USA.
Zoe MillbernDepartment of Textile Engineering, Chemistry and Science, North Carolina State University, Raleigh, NC 27695, USA.
Jonathan B GrimmJanelia Research Campus, Howard Hughes Medical Institute.
Emma C CarrollInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, CA 94158, USA; Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, USA; Department of Chemistry, San José State University, San Jose, CA 95112, USA.
K Peter R NilssonScience for Life Laboratory, KTH-Royal Institute of Technology SE-171 21 Stockholm, Sweden.
Luke D LavisJanelia Research Campus, Howard Hughes Medical Institute.
Nelson R VinuezaDepartment of Textile Engineering, Chemistry and Science, North Carolina State University, Raleigh, NC 27695, USA.
Jason E GestwickiInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, CA 94158, USA; Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, USA. Electronic address: jason.gestwicki@ucsf.edu.

Funding

Molecular Chaperones and Small MoleculesR01NS059690 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jason E Gestwicki · 2008 to 2026
$7.9M
Research Training in Chemistry and Chemical BiologyT32GM145460 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Jason E Gestwicki · 2022 to 2026
$3.1M
Differential Scanning Fluorimetry (DSF) Methods for Studying Protein StabilityR01GM141299 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GESTWICKI, JASON E · 2021 to 2024
$1.5M
Molecular recognition of pathological tau fibril conformationsF32AG076281 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CARROLL, EMMA C · 2022 to 2023
$99k
Defining the role of NC1 domain assembly in collagen biosynthesis and collagen associated disordersF31AR081704 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GALE-DAY, ZACHARY · 2023 to 2024
$82k
NIAMS NIH HHS F31 AR081704NIA NIH HHS F32 AG076281NIGMS NIH HHS R01 GM141299NIGMS NIH HHS T32 GM145460NINDS NIH HHS R01 NS059690
6 · The paper itself

Abstract

Differential Scanning Fluorimetry (DSF) is a biophysical assay that is used to estimate protein stability in vitro. In a DSF experiment, the increased fluorescence of a solvatochromatic dye, such as Sypro Orange, is used to detect the unfolding of a protein during heating. However, Sypro Orange is only compatible with a minority of proteins (< 30 %), limiting the scope of this method. We recently reported that protein-adaptive DSF (paDSF) can partially solve this problem, wherein the protein is initially pre-screened against ∼300 chemically diverse dyes, termed the Aurora collection. While this approach significantly improves the number of targets amenable to DSF, it still fails to produce protein-dye pairs for some proteins. Here, we report the expansion of the dye collection to Aurora 2.0, which includes a total of 517 structurally diverse molecules and multiple new chemotypes. To assess performance, these dyes were screened against a panel of ∼100 proteins, which were selected, in part, to represent the most challenging targets (e.g. small size). From this effort, Aurora 2.0 achieved an impressive success rate of 94 %, including producing dyes for some targets that were not matched in the original collection. These findings support the idea that larger, more chemically diverse libraries improve the likelihood of detecting melting transitions across a wider range of proteins. We propose that Aurora 2.0 makes paDSF an increasingly powerful method for studying protein stability, ligand binding and other biophysical properties in high throughput.

Indexed as

Fluorescent DyesFluorometryProteinsSmall Molecule LibrariesHumansProtein StabilityFluorescent DyesProteinsSmall Molecule LibrariesBinding assayFluorescent dyeFluorescent probesHigh throughput screeningProtein stabilityThermal shift assayThermofluor

Identifiers

PMID40784560
PMCPMC12667234

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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.