Evidence map›Paper›PMID 23106540›Full record

ArticleACS nano2012

Probing of the assembly structure and dynamics within nanoparticles during interaction with blood proteins.

Yuanpei Li, Madhu S Budamagunta, Juntao Luo, Wenwu Xiao, John C Voss, Kit S Lam

Abstract read
In one paragraph

Article in ACS nano, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Review
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  14. Extremely long tumor retention, multi-responsive boronate crosslinked micelles with superior therapeutic efficacy for ovarian cancer.Journal of controlled release : official journal of the Controlled Release Society · 2017
    Article
  15. Article
  16. Integrity of lipid nanocarriers in bloodstream and tumor quantified by near-infrared ratiometric FRET imaging in living mice.Journal of controlled release : official journal of the Controlled Release Society · 2016
    Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors.

Yuanpei LiDepartment of Biochemistry and Molecular Medicine, UC Davis Cancer Center, University of California Davis, Sacramento, California 95817, United States.
Madhu S Budamagunta
Juntao Luo
Wenwu Xiao
John C Voss
Kit S Lam

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
Therapeutic Targeting Agents for Ovarian CancerR01CA115483 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI LAM, KIT S · 2005 to 2019
$5.5M
Targeting nanotherapeutics against murine and feline oral cancerR01EB012569 · NIBIB · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LAM, KIT S · 2011 to 2019
$4.2M
Size-tunable cancer nanotherapeuticsR01CA140449 · NCI · UPSTATE MEDICAL UNIVERSITY · PI LUO, JUNTAO · 2010 to 2014
$1.6M
NCI NIH HHS P30 CA093373NCI NIH HHS R01 CA115483NCI NIH HHS R01CA115483NCI NIH HHS R01 CA140449NCI NIH HHS R01CA140449NIBIB NIH HHS R01 EB012569NIBIB NIH HHS R01EB012569
6 · The paper itself

Abstract

Fully understanding the influence of blood proteins on the assembly structure and dynamics within nanoparticles is difficult because of the complexity of the system and the difficulty in probing the diverse elements and milieus involved. Here we show the use of site-specific labeling with spin probes and fluorophores combined with electron paramagnetic resonance (EPR) spectroscopy and fluorescence resonance energy transfer (FRET) measurements to provide insights into the molecular architecture and dynamics within nanoparticles. These tools are especially useful for determining nanoparticle stability in the context of blood proteins and lipoproteins and have allowed us to quantitatively analyze the dynamic changes in assembly structure, local stability, and cargo diffusion of a class of novel telodendrimer-based micellar nanoparticles. When combined with human plasma and individual plasma components, we find that non-cross-linked nanoparticles immediately lose their original assembly structure and release their payload upon interaction with lipoproteins. In contrast, serum albumins and immunoglobulin gamma have moderate affects on the integrity of the nanoparticles. Disulfide cross-linked nanoparticles show minimal interaction with lipoproteins and can better retain their assembly structure and payload in vitro and in vivo. We further demonstrate how the enhanced stability and release property of disulfide cross-linked nanoparticles can be reversed in reductive conditions. These findings identify factors that are crucial to the performance of nanomedicines and provide design modes to control their interplay with blood factors.

Indexed as

Binding SitesBlood ProteinsHumansMaterials TestingNanoparticlesProtein BindingProtein Interaction MappingBlood Proteins

Identifiers

PMID23106540
PMCPMC3922124

What OpenQuestion holds

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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.