Evidence map›Paper›PMID 40492276›Full record

ArticleAnalytical chemistry2025

High-Throughput Analysis of Protein Adsorption to a Large Library of Polymers Using Liquid Extraction Surface Analysis-Tandem Mass Spectrometry (LESA-MS/MS).

Joris Meurs, Aishah Nasir, Grazziela P Figueredo, Laurence Burroughs, Salah A Abdelrazig, Chris Denning, David A Winkler, David A Barrett, Dong-Hyun Kim, Morgan R Alexander

Abstract read
In one paragraph

Article in Analytical chemistry, 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. Review
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

10 authors.

Joris MeursSchool of Pharmacy, University of Nottingham, Nottingham, NG7 2RD, U.K.ORCID 0000-0002-0288-0422
Aishah NasirSchool of Pharmacy, University of Nottingham, Nottingham, NG7 2RD, U.K.
Grazziela P FigueredoSchool of Computer Science, University of Nottingham, Nottingham NG8 1BB, U.K.
Laurence BurroughsSchool of Pharmacy, University of Nottingham, Nottingham, NG7 2RD, U.K.
Salah A AbdelrazigSchool of Pharmacy, University of Nottingham, Nottingham, NG7 2RD, U.K.
Chris DenningDivision of Cancer & Stem Cells, Biodiscovery Institute, University of Nottingham, Nottingham NG7 2RD, U.K.
David A WinklerSchool of Pharmacy, University of Nottingham, Nottingham, NG7 2RD, U.K.
David A BarrettSchool of Pharmacy, University of Nottingham, Nottingham, NG7 2RD, U.K.ORCID 0000-0001-6900-9474
Dong-Hyun KimSchool of Pharmacy, University of Nottingham, Nottingham, NG7 2RD, U.K.
Morgan R AlexanderSchool of Pharmacy, University of Nottingham, Nottingham, NG7 2RD, U.K.ORCID 0000-0001-5182-493X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biomaterials play an important role in medicine from contact lenses to joint replacements. High-throughput screening coupled with machine learning has identified synthetic polymers that prevent bacterial biofilm formation, prevent fungal cell attachment, control immune cell attachment and phenotype, or direct stem cell fate. In-vitro preadsorption of proteins from culture medium plays a pivotal role in controlling cell response. However, there is a paucity of studies on the screening of protein adsorption into material libraries. Here, we show how quantitative analysis of protein adsorption on a 208-member polymer microarray can be achieved using liquid extraction surface analysis, combined with an adaptation of the droplet microarray (DMA) approach and tandem mass spectrometry (LESA-MS/MS) for protein identification. This study uses a fully defined cell culture medium containing only four proteins (Essential 8) to demonstrate the feasibility of the analysis approach. Our findings show that we can generate quantitative and predictive machine learning models of protein adsorption that elucidate key polymer features that describe the relationship between surface chemistry and protein adsorption. This information is of use for the rational design of new materials with bespoke protein attachment properties for biomaterials, medical devices, or in vitro compound screening.

Indexed as

High-Throughput Screening AssaysLiquid-Liquid ExtractionPolymersProteinsTandem Mass SpectrometryAdsorptionMachine LearningSurface PropertiesPolymersProteins

Identifiers

PMID40492276
PMCPMC12199226

What OpenQuestion holds

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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.