Evidence map›Paper›PMID 42746118›Full record

ArticleChemical science2026

A resource-efficient structure-based workflow for fragment progression enables parallel hit discovery and validation of functionally diverse modulators of NCS-1 protein-protein interactions.

Daniel Muñoz-Reyes, Kate K Fieseler, Max Winokan, Mathew Golding, Eda Capkin, Matteo Ferla, Sara Pérez-Suárez, Charlie W E Tomlinson, Peter G Marples, Celia Miró-Rodríguez and 6 more

Abstract read
In one paragraph

Article in Chemical science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

16 authors.

Daniel Muñoz-ReyesDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry "Blas Cabrera", CSIC Serrano 119 Madrid 28006 Spain xmjose@iqf.csic.es.ORCID https://orcid.org/0000-0001-8464-1996
Kate K FieselerDepartment of Statistics, University of Oxford Oxford OX1 3LB UK.ORCID https://orcid.org/0000-0003-0211-8558
Max WinokanResearch Complex at Harwell, Harwell Science and Innovation Campus Didcot OX11 0FA UK frank.von-delft@diamond.ac.uk.
Mathew GoldingResearch Complex at Harwell, Harwell Science and Innovation Campus Didcot OX11 0FA UK frank.von-delft@diamond.ac.uk.ORCID https://orcid.org/0009-0004-7472-8333
Eda CapkinResearch Complex at Harwell, Harwell Science and Innovation Campus Didcot OX11 0FA UK frank.von-delft@diamond.ac.uk.
Matteo FerlaDepartment of Statistics, University of Oxford Oxford OX1 3LB UK.
Sara Pérez-SuárezDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry "Blas Cabrera", CSIC Serrano 119 Madrid 28006 Spain xmjose@iqf.csic.es.
Charlie W E TomlinsonResearch Complex at Harwell, Harwell Science and Innovation Campus Didcot OX11 0FA UK frank.von-delft@diamond.ac.uk.ORCID https://orcid.org/0000-0002-1845-6028
Peter G MarplesResearch Complex at Harwell, Harwell Science and Innovation Campus Didcot OX11 0FA UK frank.von-delft@diamond.ac.uk.
Celia Miró-RodríguezDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry "Blas Cabrera", CSIC Serrano 119 Madrid 28006 Spain xmjose@iqf.csic.es.
Lorena AguadoDepartment of Neurobiology, Instituto Ramón y Cajal de Investigación Sanitaria, Hospital Universitario Ramón y Cajal Madrid Spain.
Alicia MansillaDepartment of Neurobiology, Instituto Ramón y Cajal de Investigación Sanitaria, Hospital Universitario Ramón y Cajal Madrid Spain.ORCID https://orcid.org/0000-0002-2192-5112
Daren FearonResearch Complex at Harwell, Harwell Science and Innovation Campus Didcot OX11 0FA UK frank.von-delft@diamond.ac.uk.
Warren ThompsonResearch Complex at Harwell, Harwell Science and Innovation Campus Didcot OX11 0FA UK frank.von-delft@diamond.ac.uk.ORCID https://orcid.org/0000-0003-1474-7810
Frank von DelftResearch Complex at Harwell, Harwell Science and Innovation Campus Didcot OX11 0FA UK frank.von-delft@diamond.ac.uk.ORCID https://orcid.org/0000-0003-0378-0017
María José Sánchez-BarrenaDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry "Blas Cabrera", CSIC Serrano 119 Madrid 28006 Spain xmjose@iqf.csic.es.ORCID https://orcid.org/0000-0002-5986-1804

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Efficient drug discovery workflows ideally generate data that directly address key translational milestones, including confirmation of target engagement and binding pose, structure-activity relationships (SARs), and biological relevance, within rapid and resource-efficient experimental cycles. Here, we describe a data-driven, automation-assisted, customizable framework for fragment-to-hit progression that directly delivers structurally validated hit series primed for rapid SAR exploration by exploiting the high-throughput crystallography available at synchrotrons. This recently evolved direct-to-biology approach combines X-ray crystallographic fragment screening with algorithmically-guided fragment merging and reagent prioritization; low-cost robotic array synthesis and reaction production assessment by LC-MS; and finally orthogonal biophysical evaluation of crude reaction mixtures for binding assessment and 3D binding pose using grating-coupled interferometry and crystallography, respectively. We demonstrated the effectiveness of the strategy on a challenging target class by collectively progressing a large set of fragment hits through a single DMTA cycle comprising over 250 synthetically diverse compounds, enabling rapid, resource- and cost-effective exploration of the off-catalogue chemical space. This led to the discovery of protein-protein interaction modulators of Neuronal Calcium Sensor 1 (NCS-1), a key regulator in the central nervous system with therapeutic relevance, which contains a large interaction pocket capable of accommodating multiple protein partners. We advanced fragments into scaffold series that selectively engage biologically validated subpockets and, importantly, revealed allosteric and cryptic binding sites, critical for achieving specificity in target modulation and subsequent hit-to-lead generation. The approach is general, engineerable and scalable and provides proof of principle for how to expand the scope of fragment-based hit discovery.

Identifiers

PMID42746118
PMCPMC13575873

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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.