Evidence map›Paper›PMID 31657556›Full record

ArticleJournal of medicinal chemistry2019

Enhancing the Cell Permeability of Stapled Peptides with a Cyclic Cell-Penetrating Peptide.

Patrick G Dougherty, Jin Wen, Xiaoyan Pan, Amritendu Koley, Jian-Guo Ren, Ashweta Sahni, Ruchira Basu, Heba Salim, George Appiah Kubi, Ziqing Qian and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of medicinal chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.5field-weighted citation impact, top 4% of its field
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

34 citing papers in PubMed, 85 citations in OpenAlex.

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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

11 authors at 1 institution in 1 country.

Patrick G DoughertyDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.
Jin WenDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.
Xiaoyan PanDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.
Amritendu KoleyDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.
Jian-Guo RenEntrada Therapeutics Inc. , 50 Northern Avenue , Boston , Massachusetts 02210 , United States.
Ashweta SahniDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.
Ruchira BasuDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.
Heba SalimDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.
George Appiah KubiDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.
Ziqing QianDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.
Dehua PeiDepartment of Chemistry and Biochemistry , The Ohio State University , Columbus , Ohio 43210 , United States.ORCID 0000-0002-2057-6934
The Ohio State University · US

Funding

Development of Cell-Permeable Peptides and ProteinsR35GM122459 · NIGMS · OHIO STATE UNIVERSITY · PI Dehua Pei · 2017 to 2026
$5.1M
Macrocyclic Peptidyl Inhibitors of NEMO-IKK InteractionR01CA234124 · NCI · OHIO STATE UNIVERSITY · PI PEI, DEHUA, WANG, QIEN · 2019 to 2023
$2.1M
NCI NIH HHS R01 CA234124NIGMS NIH HHS R35 GM122459
6 · The paper itself

Abstract

Stapled peptides recapitulate the binding affinity and specificity of α-helices in proteins, resist proteolytic degradation, and may provide a novel modality against challenging drug targets such as protein-protein interactions. However, most of the stapled peptides have limited cell permeability or are impermeable to the cell membrane. We show herein that stapled peptides can be rendered highly cell-permeable by conjugating a cyclic cell-penetrating peptide to their N-terminus, C-terminus, or stapling unit. Application of this strategy to two previously reported membrane-impermeable peptidyl inhibitors against the MDM2/p53 and β-catenin/TCF interactions resulted in the generation of potent proof-of-concept antiproliferative agents against key therapeutic targets.

Indexed as

Antineoplastic Agentsbeta CateninCell Line, TumorCell Membrane PermeabilityCell-Penetrating PeptidesCell ProliferationHumansMCF-7 CellsMolecular Dynamics SimulationPeptidesPeptides, CyclicProof of Concept StudyProtein Interaction MapsProto-Oncogene Proteins c-mdm2TCF Transcription FactorsTumor Suppressor Protein p53Antineoplastic Agentsbeta CateninCell-Penetrating PeptidesCTNNB1 protein, humanMDM2 protein, humanPeptidesPeptides, CyclicProto-Oncogene Proteins c-mdm2TCF Transcription FactorsTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID31657556
PMCPMC7291828
OpenAlexW2982331182

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.