Evidence map›Paper›PMID 28370636›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2017

ROMP- and RAFT-Based Guanidinium-Containing Polymers as Scaffolds for Protein Mimic Synthesis.

Joel M Sarapas, Coralie M Backlund, Brittany M deRonde, Lisa M Minter, Gregory N Tew

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

7 citing papers in PubMed, 32 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

5 authors at 1 institution in 1 country.

Joel M SarapasDepartment of Polymer Science and Engineering, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Coralie M BacklundDepartment of Polymer Science and Engineering, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Brittany M deRondeDepartment of Polymer Science and Engineering, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Lisa M MinterDepartment of Molecular and Cellular Biology, Department of Veterinary and Animal Sciences, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Gregory N TewDepartment of Polymer Science and Engineering, University of Massachusetts Amherst, Amherst, MA, 01003, USA.ORCID http://orcid.org/0000-0003-3277-7925
University of Massachusetts Amherst · US

Funding

Targeting y-secretase in GVHDP01CA166009 · NCI · UNIVERSITY OF MASSACHUSETTS AMHERST · PI OSBORNE, BARBARA A · 2013 to 2017
$4.9M
CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
NCI NIH HHS P01 CA166009NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

Cell-penetrating peptides are an important class of molecules with promising applications in bioactive cargo delivery. A diverse series of guanidinium-containing polymeric cell-penetrating peptide mimics (CPPMs) with varying backbone chemistries was synthesized and assessed for delivery of both GFP and fluorescently tagged siRNA. Specifically, we examined CPPMs based on norbornene, methacrylate, and styrene backbones to determine how backbone structure impacted internalization of these two cargoes. Either charge content or degree of polymerization was held constant at 20, with diguanidinium norbornene molecules being polymerized to both 10 and 20 repeat units. Generally, homopolymer CPPMs delivered low amounts of siRNA into Jurkat T cells, with no apparent backbone dependence; however, by adding a short hydrophobic methyl methacrylate block to the guanidinium-rich methacrylate polymer, siRNA delivery to nearly the entire cell population was achieved. Protein internalization yielded similar results for most of the CPPMs, though the block polymer was unable to deliver proteins. In contrast, the styrene-based CPPM yielded the highest internalization for GFP (≈40 % of cells affected), showing that indeed backbone chemistry impacts protein delivery, specifically through the incorporation of an aromatic group. These results demonstrate that an understanding of how polymer structure affects cargo-dependent internalization is critical to designing new, more effective CPPMs.

Indexed as

Biocompatible MaterialsCell-Penetrating PeptidesFlow CytometryGreen Fluorescent ProteinsGuanidineHumansHydrophobic and Hydrophilic InteractionsJurkat CellsMethylmethacrylateNorbornanesPolymersRNA, Small InterferingTransfection2-norborneneBiocompatible MaterialsCell-Penetrating PeptidesGreen Fluorescent ProteinsGuanidineMethylmethacrylateNorbornanesPolymersRNA, Small Interferingbiomimicrycell-penetrating peptide mimicscontrolled polymerizationprotein deliverysiRNA

Identifiers

PMID28370636
PMCPMC5551038
OpenAlexW2599962891

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.