Evidence map›Paper›PMID 29065262›Full record

ArticleBioconjugate chemistry2017

Unlocking Endosomal Entrapment with Supercharged Arginine-Rich Peptides.

Kristina Najjar, Alfredo Erazo-Oliveras, John W Mosior, Megan J Whitlock, Ikram Rostane, Joseph M Cinclair, Jean-Philippe Pellois

Abstract read
In one paragraph

Article in Bioconjugate chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

33 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
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  5. Development and Prospects of Furin Inhibitors for Therapeutic Applications.International journal of molecular sciences · 2024
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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

7 authors at 1 institution in 1 country.

Kristina NajjarDepartment of Biochemistry and Biophysics, ⊥Program in Integrative Nutrition & Complex Diseases, Department of Nutrition and Food Science, and §Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.
Alfredo Erazo-OliverasDepartment of Biochemistry and Biophysics, ⊥Program in Integrative Nutrition & Complex Diseases, Department of Nutrition and Food Science, and §Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.
John W MosiorDepartment of Biochemistry and Biophysics, ⊥Program in Integrative Nutrition & Complex Diseases, Department of Nutrition and Food Science, and §Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.
Megan J WhitlockDepartment of Biochemistry and Biophysics, ⊥Program in Integrative Nutrition & Complex Diseases, Department of Nutrition and Food Science, and §Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.
Ikram RostaneDepartment of Biochemistry and Biophysics, ⊥Program in Integrative Nutrition & Complex Diseases, Department of Nutrition and Food Science, and §Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.
Joseph M CinclairDepartment of Biochemistry and Biophysics, ⊥Program in Integrative Nutrition & Complex Diseases, Department of Nutrition and Food Science, and §Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.
Jean-Philippe PelloisDepartment of Biochemistry and Biophysics, ⊥Program in Integrative Nutrition & Complex Diseases, Department of Nutrition and Food Science, and §Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.ORCID http://orcid.org/0000-0001-5536-925X
Texas A&M University · US

Funding

Mechanisms and optimization of endosomal escape for delivery applicationsR01GM110137 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI PELLOIS, JEAN-PHILIPPE · 2015 to 2022
$2.3M
NIGMS NIH HHS R01 GM110137
6 · The paper itself

Abstract

Endosomal entrapment is a common bottleneck in various macromolecular delivery approaches. Recently, the polycationic peptide dfTAT was identified as a reagent that induces the efficient leakage of late endosomes and, thereby, enhances the penetration of macromolecules into the cytosol of live human cells. To gain further insights into the features that lead to this activity, the role of peptide sequence was investigated. We establish that the leakage activity of dfTAT can be recapitulated by polyarginine analogs but not by polylysine counterparts. Efficiencies of peptide endocytic uptake increase linearly with the number of arginine residues present. In contrast, peptide cytosolic penetration displays a threshold behavior, indicating that a minimum number of arginines is required to induce endosomal escape. Increasing arginine content above this threshold further augments delivery efficiencies. Yet, it also leads to increasing the toxicity of the delivery agents. Together, these data reveal a relatively narrow arginine-content window for the design of optimally active endosomolytic agents.

Indexed as

ArginineAmino Acid SequenceCell-Penetrating PeptidesCytosolEndocytosisEndosomesHeLa CellsHumansArginineCell-Penetrating Peptides

Identifiers

PMID29065262
PMCPMC5905407
OpenAlexW2765607874

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.