Evidence map›Paper›PMID 27103189›Full record

ArticleBiomacromolecules2016

Optimal Hydrophobicity in Ring-Opening Metathesis Polymerization-Based Protein Mimics Required for siRNA Internalization.

Brittany M deRonde, Nicholas D Posey, Ronja Otter, Leah M Caffrey, Lisa M Minter, Gregory N Tew

Abstract read
In one paragraph

Article in Biomacromolecules, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

10 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Charge-altering releasable transporters (CARTs) for the delivery and release of mRNA in living animals.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Functional polyesters enable selective siRNA delivery to lung cancer over matched normal cells.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

6 authors at 1 institution in 1 country.

Brittany M deRondeDepartment of Polymer Science and Engineering, ‡Department of Veterinary and Animal Sciences, and §Molecular and Cellular Biology Program, University of Massachusetts Amherst , Amherst, Massachusetts 01003, United States.
Nicholas D PoseyDepartment of Polymer Science and Engineering, ‡Department of Veterinary and Animal Sciences, and §Molecular and Cellular Biology Program, University of Massachusetts Amherst , Amherst, Massachusetts 01003, United States.
Ronja OtterDepartment of Polymer Science and Engineering, ‡Department of Veterinary and Animal Sciences, and §Molecular and Cellular Biology Program, University of Massachusetts Amherst , Amherst, Massachusetts 01003, United States.
Leah M CaffreyDepartment of Polymer Science and Engineering, ‡Department of Veterinary and Animal Sciences, and §Molecular and Cellular Biology Program, University of Massachusetts Amherst , Amherst, Massachusetts 01003, United States.
Lisa M MinterDepartment of Polymer Science and Engineering, ‡Department of Veterinary and Animal Sciences, and §Molecular and Cellular Biology Program, University of Massachusetts Amherst , Amherst, Massachusetts 01003, United States.
Gregory N TewDepartment of Polymer Science and Engineering, ‡Department of Veterinary and Animal Sciences, and §Molecular and Cellular Biology Program, University of Massachusetts Amherst , Amherst, Massachusetts 01003, United States.
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

Exploring the role of polymer structure for the internalization of biologically relevant cargo, specifically siRNA, is of critical importance to the development of improved delivery reagents. Herein, we report guanidinium-rich protein transduction domain mimics (PTDMs) based on a ring-opening metathesis polymerization scaffold containing tunable hydrophobic moieties that promote siRNA internalization. Structure-activity relationships using Jurkat T cells and HeLa cells were explored to determine how the length of the hydrophobic block and the hydrophobic side chain compositions of these PTDMs impacted siRNA internalization. To explore the hydrophobic block length, two different series of diblock copolymers were synthesized: one series with symmetric block lengths and one with asymmetric block lengths. At similar cationic block lengths, asymmetric and symmetric PTDMs promoted siRNA internalization in the same percentages of the cell population regardless of the hydrophobic block length; however, with 20 repeat units of cationic charge, the asymmetric block length had greater siRNA internalization, highlighting the nontrivial relationships between hydrophobicity and overall cationic charge. To further probe how the hydrophobic side chains impacted siRNA internalization, an additional series of asymmetric PTDMs was synthesized that featured a fixed hydrophobic block length of five repeat units that contained either dimethyl (dMe), methyl phenyl (MePh), or diphenyl (dPh) side chains and varied cationic block lengths. This series was further expanded to incorporate hydrophobic blocks consisting of diethyl (dEt), diisobutyl (diBu), and dicyclohexyl (dCy) based repeat units to better define the hydrophobic window for which our PTDMs had optimal activity. High-performance liquid chromatography retention times quantified the relative hydrophobicities of the noncationic building blocks. PTDMs containing the MePh, diBu, and dPh hydrophobic blocks were shown to have superior siRNA internalization capabilities compared to their more and less hydrophobic counterparts, demonstrating a critical window of relative hydrophobicity for optimal internalization. This better understanding of how hydrophobicity impacts PTDM-induced internalization efficiencies will help guide the development of future delivery reagents.

Indexed as

Biomimetic MaterialsDrug CarriersPolymersGene Transfer TechniquesGuanidineHeLa CellsHumansHydrophobic and Hydrophilic InteractionsJurkat CellsProtein DomainsRNA InterferenceRNA, Small InterferingStructure-Activity RelationshipTransduction, GeneticDrug CarriersGuanidinePolymersRNA, Small Interfering

Identifiers

PMID27103189
PMCPMC4964964
OpenAlexW2395887891

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.