Evidence map›Paper›PMID 28269991›Full record

ArticleBiointerphases2017

Charge-transfer interactions induce surface dependent conformational changes in apolipoprotein biocorona.

Achyut J Raghavendra, Nasser Alsaleh, Jared M Brown, Ramakrishna Podila

Open access · bronzeAbstract read
In one paragraph

Article in Biointerphases, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

3 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

4 authors at 2 institutions in 1 country.

Achyut J RaghavendraLaboratory of Nano-Biophysics, Clemson Nanomaterials Center, Department of Physics and Astronomy, Clemson University, Clemson, South Carolina 29634.
Nasser AlsalehDepartment of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Science, University of Colorado-Anschutz Medical Campus, Aurora, Colorado 80045.
Jared M BrownDepartment of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Science, University of Colorado-Anschutz Medical Campus, Aurora, Colorado 80045.
Ramakrishna PodilaLaboratory of Nano-Biophysics, Clemson Nanomaterials Center, Department of Physics and Astronomy, Clemson University, Clemson, South Carolina 29634 and Center for Optical Materials Science and Engineering Technologies (COMSET), Clemson, South Carolina 29625.
Clemson University · USUniversity of Colorado Anschutz Medical Campus · US

Funding

Predicting the Toxicity of Nanomaterials by a Transforming Protein CoronaR15ES022766 · NIEHS · CLEMSON UNIVERSITY · PI RAO, APPARAO · 2014 to 2014
$445k
Nanoparticle-Protein Corona Structural Changes and ImmunoreactivityR03ES023036 · NIEHS · UNIVERSITY OF COLORADO DENVER · PI BROWN, JARED MICHAEL · 2014 to 2015
$165k
NIEHS NIH HHS R03 ES023036NIEHS NIH HHS R15 ES022766
6 · The paper itself

Abstract

Upon introduction into a biological system, engineered nanomaterials (ENMs) rapidly associate with a variety of biomolecules such as proteins and lipids to form a biocorona. The presence of "biocorona" influences nano-bio interactions considerably, and could ultimately result in altered biological responses. Apolipoprotein A-I (ApoA-I), the major constituent of high-density lipoprotein (HDL), is one of the most prevalent proteins found in ENM-biocorona irrespective of ENM nature, size, and shape. Given the importance of ApoA-I in HDL and cholesterol transport, it is necessary to understand the mechanisms of ApoA-I adsorption and the associated structural changes for assessing consequences of ENM exposure. Here, the authors used a comprehensive array of microscopic and spectroscopic tools to elucidate the interactions between ApoA-I and 100 nm Ag nanoparticles (AgNPs) with four different surface functional groups. The authors found that the protein adsorption and secondary structural changes are highly dependent on the surface functionality. Our electrochemical studies provided new evidence for charge transfer interactions that influence ApoA-I unfolding. While the unfolding of ApoA-I on AgNPs did not significantly change their uptake and short-term cytotoxicity, the authors observed that it strongly altered the ability of only some AgNPs to generate of reactive oxygen species. Our results shed new light on the importance of surface functionality and charge transfer interactions in biocorona formation.

Indexed as

AnimalsApolipoprotein A-ICell SurvivalCircular DichroismHumansMetal NanoparticlesMiceMicroscopy, Electron, TransmissionNanostructuresPolyethyleneimineProtein Structure, SecondaryRAW 264.7 CellsReactive Oxygen SpeciesSilverSurface PropertiesThioctic AcidApolipoprotein A-IPolyethyleneimineReactive Oxygen SpeciesSilverThioctic Acid

Identifiers

PMID28269991
PMCPMC5346100
OpenAlexW2594539132

What OpenQuestion holds

Textmetadata
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.