Evidence map›Paper›PMID 25314576›Full record

ArticleJournal of the American Chemical Society2014

Peptides displayed as high density brush polymers resist proteolysis and retain bioactivity.

Angela P Blum, Jacquelin K Kammeyer, Jian Yin, Dustin T Crystal, Anthony M Rush, Michael K Gilson, Nathan C Gianneschi

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.Angewandte Chemie (International ed. in English) · 2026
    Article
  4. Peptide Multifunctionalization via Modular Construction of Trans-ABAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Stimuli Induced Uptake of Protein-Like Peptide Brush Polymers.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Angela P BlumDepartment of Chemistry & Biochemistry, ‡Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego , La Jolla, California 92093, United States.
Jacquelin K Kammeyer
Jian Yin
Dustin T Crystal
Anthony M Rush
Michael K Gilson
Nathan C Gianneschi
University of Montana · USUniversity of California, San Diego · US

Funding

U of Calif, San Diego Neuroscience Microscopy ImagingP30NS047101 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GLEESON, JOSEPH G, ZHENG, BINHAI · 2003 to 2022
$9.0M
Microscopy &Image Analysis of Unstained MacromoleculesR37GM033050 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BAKER, TIMOTHY S · 2004 to 2013
$5.6M
Programming Pharmacokinetics in Vivo via In Situ Switching of Nanoscale ParticleDP2OD008724 · OD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GIANNESCHI, NATHAN CLAUDE · 2011 to 2011
$2.3M
Autonomously Assembling Nanomaterial Scaffolds for Treating Myocardial InfarctionR01HL117326 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHRISTMAN, KAREN L, GIANNESCHI, NATHAN CLAUDE · 2012 to 2016
$1.9M
EDAPT: Enzyme-Directed Assembly of Particle TheranosticsR01EB011633 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HALL, DAVID J · 2011 to 2014
$1.3M
NHLBI NIH HHS R01 HL117326NHLBI NIH HHS R01HL117326NIBIB NIH HHS 1R01EB011633NIBIB NIH HHS R01 EB011633NIGMS NIH HHS R37 GM033050NIGMS NIH HHS R37GM-033050NIH HHS 1DP2OD008724NIH HHS DP2 OD008724NINDS NIH HHS P30 NS047101
6 · The paper itself

Abstract

We describe a strategy for rendering peptides resistant to proteolysis by formulating them as high-density brush polymers. The utility of this approach is demonstrated by polymerizing well-established cell-penetrating peptides (CPPs) and showing that the resulting polymers are not only resistant to proteolysis but also maintain their ability to enter cells. The scope of this design concept is explored by studying the proteolytic resistance of brush polymers composed of peptides that are substrates for either thrombin or a metalloprotease. Finally, we demonstrate that the proteolytic susceptibility of peptide brush polymers can be tuned by adjusting the density of the polymer brush and offer in silico models to rationalize this finding. We contend that this strategy offers a plausible method of preparing peptides for in vivo use, where rapid digestion by proteases has traditionally restricted their utility.

Indexed as

ProteolysisAmino Acid SequenceCell-Penetrating PeptidesHeLa CellsHumansMolecular Dynamics SimulationNanoparticlesPeptide HydrolasesPolymersProtein ConformationProtein TransportCell-Penetrating PeptidesPeptide HydrolasesPolymers

Identifiers

PMID25314576
PMCPMC4227725
OpenAlexW2505308776

What OpenQuestion holds

Textmetadata
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.