Evidence map›Paper›PMID 29454362›Full record

ArticleJournal of nanobiotechnology2018

Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides.

Markian S Bahniuk, Abdullah K Alshememry, Scott V Elgersma, Larry D Unsworth

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of nanobiotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

6 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
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  5. Article
  6. Spontaneous Self-Organized Order Emerging From Intrinsically Disordered Protein Polymers.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology
    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

4 authors at 1 institution in 2 countries.

Markian S BahniukDepartment of Biomedical Engineering, 1098 Research Transition Facility, University of Alberta, 8308-114 Street, Edmonton, AB, T6G 2V2, Canada.ORCID http://orcid.org/0000-0002-4026-9843
Abdullah K AlshememryFaculty of Pharmacy and Pharmaceutical Sciences, 2-35B Medical Sciences Building, University of Alberta, Edmonton, AB, T6G 2H1, Canada.
Scott V ElgersmaDepartment of Chemical and Materials Engineering, University of Alberta, 12th Floor-Donadeo Innovation Centre for Engineering, 9211-116 Street, Edmonton, AB, T6G 1H9, Canada.
Larry D UnsworthDepartment of Biomedical Engineering, 1098 Research Transition Facility, University of Alberta, 8308-114 Street, Edmonton, AB, T6G 2V2, Canada. larry.unsworth@ualberta.ca.
University of Alberta · CA

Funding

Air Pollution and Asthma in Southeast LouisianaR15ES011279 · NIEHS · NICHOLLS STATE UNIVERSITY · PI ASRABADI, BADIOLLAH R · 2002 to 2002
$119k
NIEHS NIH HHS R15 ES011279
6 · The paper itself

Abstract

backgroundElastin-like polypeptides (ELPs) are a fascinating biomaterial that has undergone copious development for a variety of therapeutic applications including as a nanoscale drug delivery vehicle. A comprehensive understanding of ELP self-assembly is lacking and this knowledge gap impedes the advancement of ELP-based biomaterials into the clinical realm. The systematic examination of leucine-containing ELPs endeavors to expand existing knowledge about fundamental assembly-disassembly behaviours.

resultsIt was observed that these marginally soluble, short ELPs tend to behave consistently with previous observations related to assembly-related ELP phase transitions but deviated in their disassembly. It was found that chain length, concentration and overall sequence hydrophobicity may influence the irreversible formation of sub-micron particles as well as the formation of multi-micron scale, colloidally unstable aggregates. Amino acid composition affected surface charge and packing density of the particles. Particle stability upon dilution was found to vary depending upon chain length and hydrophobicity, with particles composed of longer and/or more hydrophobic ELPs being more resistant to disassembly upon isothermal dilution.

conclusionsTaken together, these results suggest marginally soluble ELPs may self-assemble but not disassemble as expected and that parameters including particle size, zeta potential and dilution resistance would benefit from widespread systematic evaluations. This information has the potential to reveal novel preparation methods capable of expanding the utility of all existing ELP-based biomaterials.

Indexed as

AnimalsBiocompatible MaterialsDynamic Light ScatteringElastinHumansHydrophobic and Hydrophilic InteractionsNanoparticlesParticle SizePeptidesPhase TransitionSolubilityTemperatureBiocompatible MaterialsElastinPeptidesDilution stabilityDynamic light scatteringElastin-like polypeptidesHysteresisInverse temperature transition

Identifiers

PMID29454362
PMCPMC5816514
OpenAlexW2788953387

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.