Evidence map›Paper›PMID 30063889›Full record

ArticleAnalytical biochemistry2018

Visualization of the temperature dependent rearrangement of SynB1 elastin-like polypeptide on silica using scanning electron microscopy.

Jared S Cobb, Valeria Zai-Rose, John J Correia, Amol V Janorkar

Open access · greenAbstract read
In one paragraph

Article in Analytical biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 24% 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

5 citing papers in PubMed, 6 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

4 authors at 2 institutions in 1 country.

Jared S CobbDepartment of Biomedical Materials Science, School of Dentistry, 2500 N State St, Jackson, MS, 39216, USA.
Valeria Zai-RoseDepartment of Cell and Molecular Biology, School of Medicine, University of Mississippi Medical Center, 2500 N State St, Jackson, MS, 39216, USA.
John J CorreiaDepartment of Cell and Molecular Biology, School of Medicine, University of Mississippi Medical Center, 2500 N State St, Jackson, MS, 39216, USA.
Amol V JanorkarDepartment of Biomedical Materials Science, School of Dentistry, 2500 N State St, Jackson, MS, 39216, USA. Electronic address: ajanorkar@umc.edu.
Jackson State University · USUniversity of Mississippi Medical Center · US

Funding

3D Spheroid Model of Adipose PathophysiologyR01EB020006 · NIBIB · UNIVERSITY OF MISSISSIPPI MED CTR · PI JANORKAR, AMOL VIJAY · 2016 to 2019
$1.4M
NIBIB NIH HHS R01 EB020006
6 · The paper itself

Abstract

In this study, scanning electron microscopy (SEM) was used to observe the interaction between de-solvated SynB1-elastin-like polypeptide (SynB1-ELP) and silica at a temperature above ELP's lower critical solution temperature (LCST). ELP was seen to initially wet the surface of the silica before rearranging to form narrowly distributed spherical particles. After formation, the ELP particles dynamically rearranged to increase and subsequently decrease in size until 24 h at which time they collapsed. SEM and Energy Dispersive X-ray Spectroscopy revealed that the formation of a thin layer of salt from the PBS solution preceded the initial wetting of ELP on silica, which was shown to play a role in the continuous rearrangement of ELP. FT-IR revealed that the salt, in combination with the hydrophilic silica, trapped water that provided a repulsive surface to the hydrophobic ELP and forced the ELP to continuously minimize its surface area until the water evaporated. This behavior shows that ELP's thermo-responsive nature coupled with its hydrophobicity can be used to create ELP particles and surfaces that can reorganize with minimal water present.

Indexed as

TemperatureElastinHydrophobic and Hydrophilic InteractionsMicroscopy, Electron, ScanningPeptidesSilicon DioxideSpectrometry, X-Ray EmissionElastinPeptidesSilicon DioxideAggregation kineticsDewettingElastin-like polypeptideScanning electron microscopy

Identifiers

PMID30063889
PMCPMC6129980
OpenAlexW2884061592

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.