Evidence map›Paper›PMID 34811828›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022

Stimuli Induced Uptake of Protein-Like Peptide Brush Polymers.

Angela P Blum, Jian Yin, Helen H Lin, Blayne A Oliver, Jacquelin K Kammeyer, Matthew P Thompson, Michael K Gilson, Nathan C Gianneschi

Open access · greenAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

8 authors at 3 institutions in 1 country.

Angela P BlumDepartment of Chemistry & Biochemistry, University of California San Diego, 9500 Gilman Drive, CA, 92093, La Jolla, United States.
Jian YinSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, 9500 Gilman Drive, CA, 92093, La Jolla, United States.
Helen H LinDepartment of Chemistry, Hamilton College, 198 College Hill Road, NY 13323, Clinton, United States.
Blayne A OliverDepartment of Chemistry, Hamilton College, 198 College Hill Road, NY 13323, Clinton, United States.
Jacquelin K KammeyerDepartment of Chemistry & Biochemistry, University of California San Diego, 9500 Gilman Drive, CA, 92093, La Jolla, United States.
Matthew P ThompsonDepartment of Chemistry, Department of Materials Science & Engineering, Department of Biomedical Engineering, Department of Medicine, Department of Pharmacology, International Institute of Nanotechnology, Chemistry of Life Processes Institute, Northwestern University, 633 Clark St., IL, 60208, Evanston, United States.
Michael K GilsonSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, 9500 Gilman Drive, CA, 92093, La Jolla, United States.
Nathan C GianneschiDepartment of Chemistry, Department of Materials Science & Engineering, Department of Biomedical Engineering, Department of Medicine, Department of Pharmacology, International Institute of Nanotechnology, Chemistry of Life Processes Institute, Northwestern University, 633 Clark St., IL, 60208, Evanston, United States.ORCID http://orcid.org/0000-0001-9945-5475
Hamilton College · USUniversity of California San Diego · USNorthwestern University · US

Funding

THEORY AND MODELING OF NONCOVALENT BINDINGR01GM061300 · NIGMS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI GILSON, MICHAEL K. · 2000 to 2021
$7.2M
NIGMS NIH HHS R01 GM061300NIH HHS GM61300
6 · The paper itself

Abstract

Recently, we presented a strategy for packaging peptides as side-chains in high-density brush polymers. For this globular protein-like polymer (PLP) formulation, therapeutic peptides were shown to resist proteolytic degradation, enter cells efficiently and maintain biological function. In this paper, we establish the role charge plays in dictating the cellular uptake of these peptide formulations, finding that peptides with a net positive charge will enter cells when polymerized, while those formed from anionic or neutral peptides remain outside of cells. Given these findings, we explored whether cellular uptake could be selectively induced by a stimulus. In our design, a cationic peptide is appended to a sequence of charge-neutralizing anionic amino acids through stimuli-responsive cleavable linkers. As a proof-of-concept study, we tested this strategy with two different classes of stimuli, exogenous UV light and an enzyme (a matrix metalloproteinase) associated with the inflammatory response. The key finding is that these materials enter cells only when acted upon by the stimulus. This approach makes it possible to achieve delivery of the polymers, therapeutic peptides or an appended cargo into cells in response to an appropriate stimulus.

Indexed as

PeptidesPolymersPeptide HydrolasesPolymerizationProteinsPeptide HydrolasesPeptidesPolymersProteinsBrush PolymersCell UptakeProtein-like PolymerStimuli ResponsiveTherapeutic Peptides

Identifiers

PMID34811828
PMCPMC8861929
OpenAlexW3215446587

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.