Comparative whole corona fingerprinting and protein adsorption thermodynamics of PLGA and PCL nanoparticles in human serum.
Human serum and nanoparticles
Nanoparticle protein corona
PLGA and PCL nanoparticles
Protein adsorption
Thermodynamics of protein binding
Journal
Colloids and surfaces. B, Biointerfaces
ISSN: 1873-4367
Titre abrégé: Colloids Surf B Biointerfaces
Pays: Netherlands
ID NLM: 9315133
Informations de publication
Date de publication:
Apr 2020
Apr 2020
Historique:
received:
16
06
2019
revised:
24
12
2019
accepted:
20
01
2020
pubmed:
29
1
2020
medline:
24
11
2020
entrez:
29
1
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 31991290
pii: S0927-7765(20)30046-1
doi: 10.1016/j.colsurfb.2020.110816
pmc: PMC7061085
mid: NIHMS1552215
pii:
doi:
Substances chimiques
Polyesters
0
Polylactic Acid-Polyglycolic Acid Copolymer
1SIA8062RS
polycaprolactone
24980-41-4
Serum Albumin, Human
ZIF514RVZR
Types de publication
Comparative Study
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
110816Subventions
Organisme : FIC NIH HHS
ID : K43 TW010371
Pays : United States
Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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