Evidence map›Paper›PMID 31991290›Full record

ArticleColloids and surfaces. B, Biointerfaces2020

Comparative whole corona fingerprinting and protein adsorption thermodynamics of PLGA and PCL nanoparticles in human serum.

Myolisi Ndumiso, Nela Buchtová, Lizex Husselmann, Gadija Mohamed, Ashwil Klein, Marique Aucamp, David Canevet, Sarah D'Souza, Retsepile E Maphasa, Frank Boury and 1 more

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Colloids and surfaces. B, Biointerfaces, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

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  7. Anti-Pharmaceutics · 2025
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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

11 authors at 3 institutions in 2 countries.

Myolisi NdumisoSchool of Pharmacy, University of the Western Cape, Cape Town, South Africa.
Nela BuchtováCRCINA, INSERM, Université de Nantes, Université d'Angers, Angers, France.
Lizex HusselmannDepartment of Biotechnology, University of the Western Cape, Cape Town, South Africa.
Gadija MohamedDepartment of Biotechnology, University of the Western Cape, Cape Town, South Africa.
Ashwil KleinDepartment of Biotechnology, University of the Western Cape, Cape Town, South Africa.
Marique AucampSchool of Pharmacy, University of the Western Cape, Cape Town, South Africa.
David CanevetUniversité d'Angers, Laboratoire MOLTECH-Anjou, UMR CNRS 6200, Angers, France.
Sarah D'SouzaSchool of Pharmacy, University of the Western Cape, Cape Town, South Africa.
Retsepile E MaphasaSchool of Pharmacy, University of the Western Cape, Cape Town, South Africa.
Frank BouryCRCINA, INSERM, Université de Nantes, Université d'Angers, Angers, France.
Admire DubeSchool of Pharmacy, University of the Western Cape, Cape Town, South Africa. Electronic address: adube@uwc.ac.za.
University of the Western Cape · ZAInserm · FRCentre National de la Recherche Scientifique · FR

Funding

Development of Nanomedicines for Tuberculosis TreatmentK43TW010371 · FIC · UNIVERSITY OF THE WESTERN CAPE · PI DUBE, ADMIRE · 2017 to 2021
$370k
FIC NIH HHS K43 TW010371
6 · The paper itself

Abstract

Nanoparticles (NPs) based on biocompatible and biodegradable polymers such as poly(lactic-co-glycolic acid) (PLGA) and polycaprolactone (PCL) represent effective systems for systemic drug delivery. Upon injection into the blood circuit, the NP surface is rapidly modified due to adsorption of proteins that form a 'protein corona' (PC). The PC plays an important role in cellular targeting, uptake and NP bio-distribution. Hence, the study of interactions between NPs and serum proteins appears as key for biomedical applications and safety of NPs. In the present work, we report on the comparative protein fluorescence quenching extent, thermodynamics of protein binding and identification of proteins in the soft and hard corona layers of PLGA and PCL NPs. NPs were prepared via a single emulsion-solvent evaporation technique and characterized with respect to size, zeta potential, surface morphology and hydrophobicity. Protein fluorescence quenching experiments were performed against human serum albumin. The thermodynamics of serum protein binding onto the NPs was studied using isothermal titration calorimetry. Semi-quantitative analysis of proteins in the PC layers was conducted using gel electrophoresis and mass spectrometry using human serum. Our results demonstrated the influence of particle hydrophobicity on the thermodynamics of protein binding. Human serum proteins bind to a greater extent and with greater affinity to PCL NPs than PLGA NPs. Several proteins were detected in the hard and soft corona of the NPs, representing their unique proteome fingerprints. Some proteins were unique to the PCL NPs. We anticipate that our findings will assist with rational design of polymeric NPs for effective drug delivery applications.

Indexed as

ThermodynamicsAdsorptionHumansNanoparticlesParticle SizePolyestersPolylactic Acid-Polyglycolic Acid CopolymerSerum Albumin, HumanSurface PropertiespolycaprolactonePolyestersPolylactic Acid-Polyglycolic Acid CopolymerSerum Albumin, HumanHuman serum and nanoparticlesNanoparticle protein coronaPLGA and PCL nanoparticlesProtein adsorptionThermodynamics of protein binding

Identifiers

PMID31991290
PMCPMC7061085
OpenAlexW3002802810

What OpenQuestion holds

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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.