Silver nanoparticles are one of the most important materials in the nanotechnology industry. Additionally, the protein corona is emerging as a key entity at the nanobiointerface; thus, a comprehensive understanding of the interactions between proteins and silver nanoparticles is imperative. Therefore, literature reporting studies involving both single molecule protein coronas (i.e., bovine and human serum albumin, tubulin, ubiquitin and hyaluronic-binding protein) and complex protein coronas (i.e., fetal bovine serum and yeast extract proteins) were selected to demonstrate the effects of protein coronas on silver nanoparticle cytotoxicity and antimicrobial activity. There is evidence that distinct and differential protein components may yield a "protein corona signature" that is related to the size and/or surface curvature of the silver nanoparticles. Therefore, the formation of silver nanoparticle protein coronas together with the biological response to these coronas (i.e., oxidative stress, inflammation and cytotoxicity) as well as other cellular biophysicochemical mechanisms (i.e., endocytosis, biotransformation and biodistribution) will be important for nanomedicine and nanotoxicology. Researchers may benefit from the information contained herein to improve biotechnological applications of silver nanoparticles and to address related safety concerns. In summary, the main aim of this mini-review is to highlight the relationship between the formation of silver nanoparticle protein coronas and toxicity.
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http://dx.doi.org/10.1186/s12951-015-0114-4 | DOI Listing |
Eur J Pharm Biopharm
January 2025
Department of Pharmaceutical Technology, University of Regensburg 93053 Regensburg, Bavaria, Germany. Electronic address:
The utilization of targeted nanoparticles as a selective drug delivery system is a powerful tool to increase the amount of active substance reaching the target site. This can increase therapeutic efficacy while reducing adverse drug effects. However, nanoparticles face several challenges: upon injection, the immediate adhesion of plasma proteins may mask targeting ligands, thereby diminishing the target cell selectivity.
View Article and Find Full Text PDFJ Chromatogr A
January 2025
Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, UK. Electronic address:
Research into nanoparticle interactions with biomolecules has become increasingly important in nanomedicine. While lipid nanoparticles (LNPs) are widely used as drug delivery systems, there remains a gap in understanding their fate in circulation, which is crucial for selecting appropriate lipids during formulation development. This study is the first to use Asymmetric Flow Field Flow Fractionation (AF4) to compare two types of LNPs: MC3-LNPs and SM-102-LNPs, and their interactions with a model protein, bovine serum albumin (BSA).
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
Key Laboratory of Colloid and Interface Chemistry of the Ministry of Education, School of Chemistry and Chemical Engineering, Shandong University, Jinan, Shandong 250100, China.
We report the assembly of poly(ethylene glycol) nanoparticles (PEG NPs) and optimize their surface chemistry to minimize the formation of protein coronas and immunogenicity for improved biodistribution. PEG NPs cross-linked with disulfide bonds are synthesized utilizing zeolitic imidazolate framework-8 NPs as the templates, which are subsequently modified with PEG molecules with different end groups (carboxyl, methoxy, or amino) to vary the surface chemistry. Among the modifications, the amino and residual carboxyl groups form a pair of zwitterionic structures on the surface of PEG NPs, which minimize the adsorption of proteins (e.
View Article and Find Full Text PDFFood Chem
January 2025
College of Food Science and Engineering, Qingdao Agricultural University, Qingdao, Shandong Province, 266109, China; Qingdao Special Food Research Institute, Qingdao, 266109, China. Electronic address:
This study investigates the interaction of amino-modified starch nanoparticles (NH-SNPs) and unmodified SNPs with pepsin and trypsin and the influence of the formation of protein coronas on the release of polyphenols. We discovered that NH-SNPs bound loosely to pepsin, while they bound tightly to trypsin, by quartz crystal microbalance with dissipation monitoring and zeta potential measurement. SNPs did not easily bind to the two digestive enzymes.
View Article and Find Full Text PDFACS Pharmacol Transl Sci
January 2025
Fraunhofer Institute for Translational Medicine and Pharmacology ITMP, Discovery Research ScreeningPort, Schnackenburgallee 114, 22525 Hamburg, Germany.
The SARS-CoV-2 papain-like protease PLpro has multiple roles in the viral replication cycle, related to both its polypeptide cleavage function and its ability to antagonize the host immune response. Targeting the PLpro function is recognized as a promising mechanism to modulate viral replication, while supporting host immune responses. However, the development of PLpro-specific inhibitors remains challenging.
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