Evidence map›Paper›PMID 42457721›Full record

ArticleNature communications2026

ADAPT-M: a workflow for rapid, quantitative in vitro measurements of enriched protein libraries.

Carla P Perez, Nicole V DelRosso, Cameron L Noland, Udit Parekh, Christian A Choe, Raphael R Eguchi, Qi Wen, Polly M Fordyce, Po-Ssu Huang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Amplicon/Protein Bead Display enables quantitativebioRxiv : the preprint server for biology · 2026
    Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Carla P Perez *Biophysics Program, Stanford University, Stanford, CA, USA.
Nicole V DelRosso *Biophysics Program, Stanford University, Stanford, CA, USA. nicole.delrosso@ucsf.edu.
Cameron L NolandDiscovery Chemistry, Merck & Co. Inc., South San Francisco, CA, USA.
Udit ParekhDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
Christian A ChoeDepartment of Bioengineering, Stanford University, Stanford, CA, USA.ORCID http://orcid.org/0000-0001-8871-9682
Raphael R EguchiDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
Qi WenDepartment of Bioengineering, Stanford University, Stanford, CA, USA.ORCID http://orcid.org/0009-0007-3731-6163
Polly M FordyceBiophysics Program, Stanford University, Stanford, CA, USA. pfordyce@stanford.edu.ORCID http://orcid.org/0000-0002-9505-0638
Po-Ssu HuangBiophysics Program, Stanford University, Stanford, CA, USA. possu@stanford.edu.ORCID http://orcid.org/0000-0002-7948-2895

Funding

Using microfluidics to realize patient-specific anti-cancer immunotherapiesDP1CA290563 · NCI · STANFORD UNIVERSITY · PI Polly Morrell Fordyce · 2023 to 2026
$5.4M
Stanford Chem-H Chemistry/Biology Interface Predoctoral Training ProgramT32GM120007 · NIGMS · STANFORD UNIVERSITY · PI BERTOZZI, CAROLYN · 2016 to 2020
$1.2M
American Diabetes Association (ADA) 9-22-PDFPM-05Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) DP1CA290563National Science Foundation (NSF) CAREER 2142336NCI NIH HHS DP1 CA290563NIGMS NIH HHS T32 GM120007U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) T32GM120007
6 · The paper itself

Abstract

Protein-protein interactions underpin most cellular processes, and engineered binders present powerful tools for probing biology and developing novel therapeutics. However, scalable, quantitative characterization of large numbers of candidates remains a major bottleneck. Here we show that ADAPT-M (Affinity Determination by Adaptation of ProTein binders for Microfluidics) enables rapid, parallel measurement of binding affinities and dissociation behavior directly from enriched display libraries in under one week, without requiring gene synthesis or hands-on protein purification. Applied to a computationally designed library targeting the SARS-CoV-2 Omicron BA.1 receptor binding domain, ADAPT-M recovered most highly enriched variants and revealed that many display-enriched binders lacked measurable binding in vitro, highlighting limitations of screening alone. ADAPT-M enabled quantitative characterization of dozens of binders in parallel and selection of lead candidates for structural analysis. Unexpectedly, structural and mutational studies revealed that designed binding interfaces were preserved despite engaging alternative epitopes. By bridging screening and scalable in vitro validation, ADAPT-M accelerates protein binder discovery and supports data-driven protein engineering.

Indexed as

Peptide LibrarySARS-CoV-2COVID-19HumansMicrofluidicsProtein BindingProtein EngineeringWorkflowPeptide Library

Identifiers

PMID42457721
PMCPMC13490508

What OpenQuestion holds

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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.