Evidence map›Paper›PMID 40852896›Full record

ArticleProtein science : a publication of the Protein Society2025

Using extension-based mRNA display to design antibody-like proteinogenic peptides for human PD-L1.

Justin N Ong, Brian J Grindel, Scott A Rankin, Sarah H Naylon, Anupallavi Srinivasamani, Guillaume J Trusz, Xiaowen Liang, Md Nasir Uddin, Lauren Fuller, Michael Curran and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 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
  2. Article
  3. 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

14 authors.

Justin N OngDeparment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Brian J GrindelDeparment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Scott A RankinDepartment of Chemistry, University of Southern California, Los Angeles, California, USA.
Sarah H NaylonDepartment of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, Florida, USA.
Anupallavi SrinivasamaniDepartment of Immunology, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Guillaume J TruszDepartment of Immunology, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Xiaowen LiangDepartment of Experimental Therapeutics, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Md Nasir UddinDeparment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Lauren FullerDeparment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Michael CurranDepartment of Immunology, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Stephane P RocheDepartment of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, Florida, USA.
Terry T TakahashiDepartment of Chemistry, University of Southern California, Los Angeles, California, USA.
Richard W RobertsMork Family Department of Chemical Engineering and Materials Science, University of Southern California, Los Angeles, California, USA.
Steven W MillwardDeparment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.ORCID 0000-0002-3231-7075

Funding

G.E. In-kind Multi-Investigator Imaging (MI2) Research AwardMD Anderson Institutional Research GrantMD Anderson Quantitative Imaging Analysis Core Partnership in Research Program Pilot Award
6 · The paper itself

Abstract

Many peptide drugs rely on nonproteinogenic amino acids and chemical modifications for improved activity and proteolytic stability. However, these features also make drug production expensive and challenging to scale. Here, we engineered small, linear, proteinogenic peptides that bind human programmed death-ligand 1 (hPD-L1) with high affinity and stability using mRNA display affinity maturation. The resulting peptides, SPAM2 and SPAM3, have antibody-like affinities for hPD-L1 (dissociation constants between ~250 and 300 pM) and are selective for hPD-L1. Both SPAM2 and SPAM3 compete with hPD-L1 ligands known to interact with the programmed cell death protein 1 site and are stable in human serum. SPAM3 bound human glioma D423 cells with high affinity in flow cytometry experiments comparable to that of a clinical therapeutic antibody. These results support the use of affinity maturation selections to dramatically enhance the biophysical properties of linear, proteinogenic peptides for translational applications.

Indexed as

B7-H1 AntigenPeptidesRNA, MessengerCell Line, TumorHumansProtein EngineeringB7-H1 AntigenCD274 protein, humanPeptidesRNA, Messengeraffinity maturationimmune checkpointmRNA displayPD‐L1peptide

Identifiers

PMID40852896
PMCPMC12376068

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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.