Evidence map›Paper›PMID 41875055›Full record

ArticleJournal of medicinal chemistry2026

Yeast Display Technology Enables Rapid Discovery of Low-Nanomolar Macrocyclic Peptide Inhibitors of Human Angiotensin-Converting Enzyme 2.

Zhanna Romanyuk, Giacomo Bettin, Paul Brear, Sara Linciano, Ylenia Mazzocato, Simone Bonadies, Ilaria Zanotto, Camilla Mazzucco, Alan Monferone, Miguel A Soler and 7 more

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Article in Journal of medicinal chemistry, 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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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

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

17 authors.

Zhanna RomanyukDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Mestre, Italy.
Giacomo BettinArzanya S.r.l., Via Rezzonico 6, 35131 Padua, Italy.ORCID 0009-0003-3511-6679
Paul BrearDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, U.K.ORCID 0000-0002-4045-0474
Sara LincianoDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Mestre, Italy.
Ylenia MazzocatoDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Mestre, Italy.
Simone BonadiesDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Mestre, Italy.
Ilaria ZanottoDepartment of Pharmaceutical and Pharmacological Sciences, University of Padua, Via F. Marzolo 5, 35131 Padua, Italy.
Camilla MazzuccoDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Mestre, Italy.
Alan MonferoneDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Mestre, Italy.
Miguel A SolerDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Mestre, Italy.
Gianfranco PasutDepartment of Pharmaceutical and Pharmacological Sciences, University of Padua, Via F. Marzolo 5, 35131 Padua, Italy.ORCID 0000-0002-8754-0899
Sara De MartinDepartment of Pharmaceutical and Pharmacological Sciences, University of Padua, Via F. Marzolo 5, 35131 Padua, Italy.
Alessandro ScarsoDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Mestre, Italy.ORCID 0000-0001-6114-9181
Christian HeinisInstitute of Chemical Sciences and Engineering, School of Basic Sciences, École Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland.ORCID 0000-0001-9982-9457
Sylvia RothenbergerInstitute of Microbiology, University Hospital Center and University of Lausanne, Rue du Bugnon 48, 1011 Lausanne, Switzerland.
Marko HyvönenDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, U.K.ORCID 0000-0001-8683-4070
Alessandro AngeliniDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Mestre, Italy.ORCID 0000-0001-5923-3843

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Macrocyclic peptides (MPs) are valuable molecular formats for drug development, bridging small molecules and larger biologics due to their favorable pharmacological properties. Here, we describe the discovery of low-nanomolar inhibitors of human angiotensin-converting enzyme 2 (hACE2) by quantitatively screening millions of structurally diverse disulfide-cyclized peptide ligands using yeast display technology. The most potent yeast-encoded "one-ring" and "two-ring" MP inhibit hACE2 with

Indexed as

Angiotensin-Converting Enzyme InhibitorsDrug DiscoveryMacrocyclic CompoundsPeptides, CyclicPeptidyl-Dipeptidase ASaccharomyces cerevisiaeAngiotensin-Converting Enzyme 2Crystallography, X-RayHumansModels, MolecularStructure-Activity RelationshipACE2 protein, humanAngiotensin-Converting Enzyme 2Angiotensin-Converting Enzyme InhibitorsMacrocyclic CompoundsPeptides, CyclicPeptidyl-Dipeptidase A

Identifiers

PMID41875055
PMCPMC13071878

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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.