Evidence map›Paper›PMID 30533583›Full record

ArticleACS omega2018

Enhanced Fluorescent Protein Activity in Polymer Scaffold-Stabilized Phospholipid Nanoshells Using Neutral Redox Initiator Polymerization Conditions.

Surajit Ghosh, Xuemin Wang, Jinyan Wang, Phuong-Diem Nguyen, Colleen M Janczak, Craig A Aspinwall

Abstract read
In one paragraph

Article in ACS omega, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Surajit GhoshDepartment of Chemistry and Biochemistry, BIO5 Institute, and Department of Biomedical Engineering, The University of Arizona, Tucson, Arizona 85721, United States.
Xuemin WangDepartment of Chemistry and Biochemistry, BIO5 Institute, and Department of Biomedical Engineering, The University of Arizona, Tucson, Arizona 85721, United States.
Jinyan WangDepartment of Chemistry and Biochemistry, BIO5 Institute, and Department of Biomedical Engineering, The University of Arizona, Tucson, Arizona 85721, United States.
Phuong-Diem NguyenDepartment of Chemistry and Biochemistry, BIO5 Institute, and Department of Biomedical Engineering, The University of Arizona, Tucson, Arizona 85721, United States.
Colleen M JanczakDepartment of Chemistry and Biochemistry, BIO5 Institute, and Department of Biomedical Engineering, The University of Arizona, Tucson, Arizona 85721, United States.
Craig A AspinwallDepartment of Chemistry and Biochemistry, BIO5 Institute, and Department of Biomedical Engineering, The University of Arizona, Tucson, Arizona 85721, United States.

Funding

Sniffer Biosensors Based on Ion Channel-GPCR Chimeras and Polylipid MembranesR01EB007047 · NIBIB · UNIVERSITY OF ARIZONA · PI ASPINWALL, CRAIG A, SAAVEDRA, STEVEN SCOTT · 2006 to 2015
$3.5M
Nanoshell sensors for cellular analysisR01GM116946 · NIGMS · UNIVERSITY OF ARIZONA · PI ASPINWALL, CRAIG A · 2015 to 2018
$1.2M
Stabilized Biomimetic Separation MediaR01GM095763 · NIGMS · UNIVERSITY OF ARIZONA · PI ASPINWALL, CRAIG A · 2011 to 2014
$1.1M
NIBIB NIH HHS R01 EB007047NIGMS NIH HHS R01 GM095763NIGMS NIH HHS R01 GM116946
6 · The paper itself

Abstract

Phospholipid nanoshells, for example, liposomes, provide a versatile enabling platform for the development of nanometer-sized biosensors and molecular delivery systems. Utilization of phospholipid nanoshells is limited by the inherent instability in complex biological environments, where the phospholipid nanoshell may disassemble and degrade, thus releasing the contents and destroying sensor function. Polymer scaffold stabilization (PSS), wherein the phospholipid nanoshells are prepared by partitioning reactive monomers into the lipid bilayer lamella followed by radical polymerization, has emerged to increase phospholipid nanoshell stability. In this work, we investigated the effects of three different radical initiator conditions to fabricate stable PSS-phospholipid nanoshells yet retain the activity of encapsulated model fluorescent sensor proteins. To identify nondestructive initiation conditions, UV photoinitiation, neutral redox initiation, and thermal initiation were investigated as a function of PSS-phospholipid nanoshell stabilization and fluorescence emission intensity of enhanced green fluorescent protein (eGFP) and tandem dimer Tomato (td-Tomato). All three initiator approaches yielded comparably stable PSS-phospholipid nanoshells, although slight variations in PSS-phospholipid nanoshell size were observed, ranging from ca. 140 nm for unstabilized phospholipid nanoshells to 300-500 nm for PSS-phospholipid nanoshells. Fluorescence emission intensity of encapsulated eGFP was completely attenuated under thermal initiation (0% vs control), moderately attenuated under UV photoinitiation (40 ± 4% vs control), and unaffected by neutral redox initiation (97 ± 3% vs control). Fluorescence emission intensity of encapsulated td-Tomato was significantly attenuated under thermal initiation (13 ± 3% vs control), moderately attenuated UV photoinitiation (64 ± 5% vs control), and unaffected by neutral redox initiation (98% ± 4% vs control). Therefore, the neutral redox initiation method provides a significant advancement toward the preparation of protein-functionalized PSS-phospholipid nanoshells. These results should help to guide future applications and designs of biosensor platforms using PSS-phospholipid nanoshells and other polymer systems employing protein transducers.

Identifiers

PMID30533583
PMCPMC6276202

What OpenQuestion holds

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Registered trials

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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.