Identification of main influencing factors on the protein corona composition of PLGA and PLA nanoparticles

Spreen, Hendrik; Behrens, Matthias; Mulac, Dennis; Humpf, Hans‐Ulrich; Langer, Klaus

doi:10.1016/j.ejpb.2021.04.006

Cited by 15 publications

(4 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Due to their acidic nature, PLGA monomers are not directly suitable for use in medicines or bioactive compounds. To address this challenge, various approaches have been developed, including the use of ingredients like alginate [ 38 ], chitosan [ 39 ], poly(vinyl alcohol) [ 40 ], and others to prepare PLGA nanomedicine formulations. Recognized as a safe material by the US Food and Drug Administration (FDA), PLGA has seen the development and commercialization of numerous medications for a variety of ailments, with several agents effectively loaded into PLGA nanoparticles or bonded to them [ 41 ].…”

Section: Nature and Chemistry Of Pnps And Nanogelsmentioning

confidence: 99%

Polymeric Nanoparticles and Nanogels: How Do They Interact with Proteins?

Sadeghi,

PourEskandar,

Askari

et al. 2023

Gels

View full text Add to dashboard Cite

Polymeric nanomaterials, nanogels, and solid nanoparticles can be fabricated using single or double emulsion methods. These materials hold great promise for various biomedical applications due to their biocompatibility, biodegradability, and their ability to control interactions with body fluids and cells. Despite the increasing use of nanoparticles in biomedicine and the plethora of publications on the topic, the biological behavior and efficacy of polymeric nanoparticles (PNPs) have not been as extensively studied as those of other nanoparticles. The gap between the potential of PNPs and their applications can mainly be attributed to the incomplete understanding of their biological identity. Under physiological conditions, such as specific temperatures and adequate protein concentrations, PNPs become coated with a “protein corona” (PC), rendering them potent tools for proteomics studies. In this review, we initially investigate the synthesis routes and chemical composition of conventional PNPs to better comprehend how they interact with proteins. Subsequently, we comprehensively explore the effects of material and biological parameters on the interactions between nanoparticles and proteins, encompassing reactions such as hydrophobic bonding and electrostatic interactions. Moreover, we delve into recent advances in PNP-based models that can be applied to nanoproteomics, discussing the new opportunities they offer for the clinical translation of nanoparticles and early prediction of diseases. By addressing these essential aspects, we aim to shed light on the potential of polymeric nanoparticles for biomedical applications and foster further research in this critical area.

show abstract

Section: Nature and Chemistry Of Pnps And Nanogelsmentioning

confidence: 99%

Polymeric Nanoparticles and Nanogels: How Do They Interact with Proteins?

Sadeghi,

PourEskandar,

Askari

et al. 2023

Gels

View full text Add to dashboard Cite

show abstract

“…This process usually generates two layers of proteins that are adsorbed onto the NPs' surface, namely hard and soft corona. The analysis and isolation of such adsorbed proteins have revealed that corona composition may change over time until reaching an equilibrium state [60] and is mainly composed of abundant proteins such as albumin and other less abundant ones that tend to interact selectively with the NPs' surface [41,61]. Interestingly, the presence of this corona layer may produce significant changes in their biological activity affecting the long-term fate of NPs.…”

Section: Protein Corona (Pc)mentioning

confidence: 99%

“…Consequently, a full understanding of the effect of such corona on the stability of NPs is essential for the appropriate design of nanotherapeutics. The formation of PC NPs between polymeric NPs (e.g., PLGA and PLGA-PEG) with plasma proteins (FBS), their biophysical characterization, and isolation have been reported [60,[62][63][64][65][66]. In these studies, NPs were mainly prepared via solvent emulsification-diffusion methods [66] using PVA as a stabilizer together with the use of high-energy methods (e.g., ultracentrifugation or high-speed homogenizer).…”

Section: Protein Corona (Pc)mentioning

confidence: 99%

Rosmarinic Acid-Loaded Polymeric Nanoparticles Prepared by Low-Energy Nano-Emulsion Templating: Formulation, Biophysical Characterization, and In Vitro Studies

et al. 2022

View full text Add to dashboard Cite

Rosmarinic acid (RA), a caffeic acid derivative, has been loaded in polymeric nanoparticles made up of poly(lactic-co-glycolic acid) (PLGA) through a nano-emulsion templating process using the phase-inversion composition (PIC) method at room temperature. The obtained RA-loaded nanoparticles (NPs) were colloidally stable exhibiting average diameters in the range of 70–100 nm. RA was entrapped within the PLGA polymeric network with high encapsulation efficiencies and nanoparticles were able to release RA in a rate-controlled manner. A first-order equation model fitted our experimental data and confirmed the prevalence of diffusion mechanisms. Protein corona formation on the surface of NPs was assessed upon incubation with serum proteins. Protein adsorption induced an increase in the hydrodynamic diameter and a slight shift towards more negative surface charges of the NPs. The radical scavenging activity of RA-loaded NPs was also studied using the DPPH·assay and showed a dose–response relationship between the NPs concentration and DPPH inhibition. Finally, RA-loaded NPs did not affect the cellular proliferation of the human neuroblastoma SH-SY5Y cell line and promoted efficient cellular uptake. These results are promising for expanding the use of O/W nano-emulsions in biomedical applications.

show abstract

“…For instance, when preparing nanoparticles from poly(D,L-lactide-co-glycolide) (PLGA) and, alternatively, from its diblock copolymer with poly(ethylene glycol) (PEG-PLGA), a lower protein adsorption was found for PEG-PLGA, presumably due to hydrophilic PEG-rich domains being present at the particle surface [11]. Furthermore, despite similar coverage of PLGA particles with surfactant, more hydrophilic PLGA with free carboxyl groups adsorbed almost tenfold more protein than more hydrophobic ethyl end-capped PLGA, suggesting that ionic interactions might dominate over hydrophobic interactions in certain cases [12]. In addition to those observations with individual materials, it would be of interest to realize polymer-composition-dependent control of protein adsorption processes by a series of materials with tunable composition and thereby tunable protein adsorption.…”

Section: Introductionmentioning

confidence: 99%

Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-co-styrene) Nanoparticle Series

Seifert,

Baudis,

Wischke

2023

IJMS

View full text Add to dashboard Cite

Polymer nanoparticles continue to be of high interest in life science applications. Still, adsorption processes occurring in protein-containing media and their implications for biological responses are not generally predictable. Here, the effect of nanoparticle composition on the adsorption of bovine serum albumin (BSA), fibronectin (FN) and immunoglobulin G (IgG) as structurally and functionally different model proteins was explored by systematically altering the composition of poly(methyl methacrylate-co-styrene) nanoparticles with sizes in a range of about 550 nm. As determined by protein depletion from the suspension medium via a colorimetric assay, BSA and IgG adsorbed at similar quantities, while FN reached larger masses of adsorbed protein (up to 0.4 ± 0.06 µg·cm−2 BSA, 0.42 ± 0.09 µg·cm−2 IgG, 0.72 ± 0.04 µg·cm−2 FN). A higher content of styrene as the more hydrophobic polymer component enhanced protein binding, which suggests a contribution of hydrophobic interactions despite the particles exhibiting strongly negatively charged surfaces with zeta potentials of −44 to −52 mV. The quantities of adsorbed proteins were estimated to correspond to a confluent surface coverage. Overall, this study illustrated how protein binding can be controlled by systematically varying the nanoparticle bulk composition and may serve as a basis for establishing interfaces with a targeted level of protein retention and/or presentation.

show abstract

Identification of main influencing factors on the protein corona composition of PLGA and PLA nanoparticles

Cited by 15 publications

References 49 publications

Polymeric Nanoparticles and Nanogels: How Do They Interact with Proteins?

Polymeric Nanoparticles and Nanogels: How Do They Interact with Proteins?

Rosmarinic Acid-Loaded Polymeric Nanoparticles Prepared by Low-Energy Nano-Emulsion Templating: Formulation, Biophysical Characterization, and In Vitro Studies

Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-co-styrene) Nanoparticle Series

Contact Info

Product

Resources

About