Evidence map›Paper›PMID 26051652›Full record

ArticleNanomedicine : nanotechnology, biology, and medicine2015

Optimizing the design of protein nanoparticles as carriers for vaccine applications.

Tais A P F Doll, Tobias Neef, Nha Duong, David E Lanar, Philippe Ringler, Shirley A Müller, Peter Burkhard

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nanomedicine : nanotechnology, biology, and medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

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  15. Design and optimization of peptide nanoparticles.Journal of nanobiotechnology · 2015
    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

7 authors.

Tais A P F DollInstitute of Materials Science, University of Connecticut, Storrs, CT, USA.
Tobias NeefDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA.
Nha DuongDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA.
David E LanarMalaria Vaccine Branch, Walter Reed Army Institute of Research, Silver Spring, Maryland, MD, USA.
Philippe RinglerCenter for Cellular Imaging and Nano Analytics (C-CINA), Biozentrum, University of Basel, Mattenstrasse 26, Basel, Switzerland.
Shirley A MüllerCenter for Cellular Imaging and Nano Analytics (C-CINA), Biozentrum, University of Basel, Mattenstrasse 26, Basel, Switzerland.
Peter BurkhardInstitute of Materials Science, University of Connecticut, Storrs, CT, USA; Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA. Electronic address: peter.burkhard@uconn.edu.

Funding

Structural basis of the specific protein-protein interactions underlying IF assemP01GM096971 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI JANMEY, PAUL A · 2011 to 2021
$16.8M
A Peptide Nanoparticle Nicotine VaccineDP1DA033524 · NIDA · UNIVERSITY OF CONNECTICUT STORRS · PI BURKHARD, PETER · 2011 to 2015
$3.9M
Malaria Vaccine Based on Self-Assembling Polypeptide Nanoparticles (SAPN)R01AI068761 · NIAID · UNIVERSITY OF CONNECTICUT STORRS · PI BURKHARD, PETER, LANAR, DAVID ERVIN · 2009 to 2012
$2.1M
NIAID NIH HHS 5R01AI068761NIAID NIH HHS R01 AI068761NIDA NIH HHS 1DP1DA033524NIDA NIH HHS DP1 DA033524NIGMS NIH HHS 1P01GM096971NIGMS NIH HHS P01 GM096971
6 · The paper itself

Abstract

Successful vaccine development remains a huge challenge for infectious diseases such as malaria, HIV and influenza. As a novel way to present antigenic epitopes to the immune system, we have developed icosahedral self-assembling protein nanoparticles (SAPNs) to serve as a prototypical vaccine platform for infectious diseases. Here we examine some biophysical factors that affect the self-assembly of these nanoparticles, which have as basic building blocks coiled-coil oligomerization domains joined by a short linker region. Relying on in silico computer modeling predictions, we selected five different linker regions from the RCSB protein database that connect oligomerization domains, and then further studied the self-assembly and stability of in vitro produced nanoparticles through biophysical characterization of formed particles. One design in particular, T2i88, revealed excellent self-assembly and homogeneity thus paving the way toward a more optimized nanoparticle for vaccine applications. FROM THE CLINICAL EDITOR: Despite the widespread use of vaccines worldwide, successful development of vaccines against some diseases remains a challenge still. In this article, the authors investigated the physic-chemical and biological properties of icosahedral self-assembling protein nanoparticles (SAPNs), which mimic viral particles, in order to utilize this technology as potential platform for future design of vaccines.

Indexed as

Computer SimulationDatabases, ProteinHIV InfectionsHumansInfluenza, HumanMalariaNanoparticlesProteinsVaccinesProteinsVaccinesMalariaProtein designProtein nanoparticleSelf-assemblyVaccine carrier

Identifiers

PMID26051652
PMCPMC4587294

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.