Evidence map›Paper›PMID 39611613›Full record

ArticleThe Journal of organic chemistry2025

Advancements in Loop Cyclization Approaches for Enhanced Peptide Therapeutics for Targeting Protein-Protein Interactions.

Lucia Lombardi, Luke A Granger, Robin J Shattock, Daryl R Williams

Abstract read
In one paragraph

Article in The Journal of organic 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

4 authors.

Lucia LombardiDepartment of Chemical Engineering, South Kensington Campus, Imperial College London, London SW7 2AZ, U.K.ORCID 0000-0002-5202-9847
Luke A GrangerDepartment of Infectious Disease, South Kensington Campus, Imperial College London, London SW7 2AZ, U.K.
Robin J ShattockDepartment of Infectious Disease, South Kensington Campus, Imperial College London, London SW7 2AZ, U.K.
Daryl R WilliamsDepartment of Chemical Engineering, South Kensington Campus, Imperial College London, London SW7 2AZ, U.K.ORCID 0000-0001-5626-5903

Funding

EPSRC EP/T005556/1Wellcome Trust
6 · The paper itself

Abstract

Protein-protein interactions (PPIs) are pivotal in regulating cellular functions and life processes, making them promising therapeutic targets in modern medicine. Despite their potential, developing PPI inhibitors poses significant challenges due to their large and shallow interfaces that complicate ligand binding. This study focuses on mimicking peptide loops as a strategy for PPI inhibition, utilizing synthetic peptide loops for replicating critical binding regions. This work explores turn-inducing elements and highlights the importance of proline in promoting favorable conformations for lactamization, yielding high-purity cyclic peptides. Notably, our one-pot method offers enhanced versatility and represents a robust strategy for efficient and selective macrolactamization, expanding the scope of peptide synthesis methodologies. This approach, validated through the synthesis of AAV capsid-derived loops, offers a robust platform for developing peptide-based therapeutics and highlights the potential of peptide macrocycles in overcoming PPI drug discovery challenges and advancing the development of new therapeutics.

Indexed as

PeptidesPeptides, CyclicCyclizationHumansMolecular StructureProtein BindingPeptidesPeptides, Cyclic

Identifiers

PMID39611613
PMCPMC11791882

What OpenQuestion holds

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LicenceCC BY
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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.