Evidence map›Paper›PMID 31276085›Full record

ArticlePeptide science (Hoboken, N.J.)2019

CPProtectides: Rapid uptake of well-folded β-hairpin peptides with enhanced resistance to intracellular degradation.

Nora Safa, Jeffery C Anderson, Manibarathi Vaithiyanathan, Jacob H Pettigrew, Gavin A Pappas, Dong Liu, Ted J Gauthier, Adam T Melvin

Open access · greenAbstract read
In one paragraph

Article in Peptide science (Hoboken, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Stapled β-Hairpins Featuring 4-Mercaptoproline.Journal of the American Chemical Society · 2021
    Article
  7. Article
  8. Assay Systems for Profiling Deubiquitinating Activity.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. 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

8 authors at 1 institution in 1 country.

Nora SafaCain Department of Chemical Engineering, Louisiana State University, Baton Rouge, Louisiana.
Jeffery C AndersonCain Department of Chemical Engineering, Louisiana State University, Baton Rouge, Louisiana.
Manibarathi VaithiyanathanCain Department of Chemical Engineering, Louisiana State University, Baton Rouge, Louisiana.
Jacob H PettigrewCain Department of Chemical Engineering, Louisiana State University, Baton Rouge, Louisiana.
Gavin A PappasCain Department of Chemical Engineering, Louisiana State University, Baton Rouge, Louisiana.
Dong LiuLSU AgCenter Biotechnology Lab, Louisiana State University, Baton Rouge, Louisiana.
Ted J GauthierLSU AgCenter Biotechnology Lab, Louisiana State University, Baton Rouge, Louisiana.
Adam T MelvinCain Department of Chemical Engineering, Louisiana State University, Baton Rouge, Louisiana.ORCID 0000-0003-0484-5871
Louisiana State University · US

Funding

Ex vivo analysis of deubiquitinating enzyme activity in single multiple myeloma cellsR03EB020935 · NIBIB · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI MELVIN, ADAM THOMAS · 2015 to 2016
$140k
NIBIB NIH HHS R03 EB020935
6 · The paper itself

Abstract

Cell penetrating peptides (CPPs) have emerged as powerful tools for delivering bioactive cargoes, such as biosensors or drugs to intact cells. One limitation of CPPs is their rapid degradation by intracellular proteases. β-hairpin "protectides" have previously been demonstrated to be long-lived under cytosolic conditions due to their secondary structure. The goal of this work was to demonstrate that arginine-rich β-hairpin peptides function as both protectides and as CPPs. Peptides exhibiting a β-hairpin motif were found to be rapidly internalized into cells with their uptake efficiency dependent on the number of arginine residues in the sequence. Cellular internalization of the β-hairpin peptides was compared to unstructured, scrambled sequences and to commercially available, arginine-rich CPPs. The unstructured peptides displayed greater uptake kinetics compared to the structured β-hairpin sequences; however, intracellular stability studies revealed that the β-hairpin peptides exhibited superior stability under cytosolic conditions with a 16-fold increase in peptide half-life. This study identifies a new class of long-lived CPPs that can overcome the stability limitations of peptide-based reporters or bioactive delivery mechanisms in intact cells.

Indexed as

cell penetrating peptideprotectideβ-hairpin

Identifiers

PMID31276085
PMCPMC6605100
OpenAlexW2894377561

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.