Bimetallic coating over gold nanorods improves biocorona formation, enhances drug loading and release, and reduces non-specific in vitro toxicity.

Chandra Sekaran N

Centre for Nanobiotechnology

Vellore Campus

Amitava Mukherjee

Chakraborty D

Mohan L

Alex S.A

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

&nbsp;

&nbsp;

VIT University

Biomaterials Science

Incorporation of nanoparticles in serum containing-media leads to spontaneous adsorption of proteins on the nanoparticle surface thus forming “protein corona”. The current study focuses on the variation in corona formation across differently functionalized (CTAB, SDS and Brij-58) SeNPs surfaces and the application of these coronated-SeNPs as reservoirs for holding positively charged doxorubicin (dox). Protein quantification and densitometry study reveal that cationic SeNPs (CTAB-SeNPs) promotes maximum corona formation, and also has a higher affinity towards predominantly negatively charged serum albumin. Further, protein coronation had a significant impact on the mean hydrodynamic diameter of the functionalized SeNPs. Parameters such as surface functionalization, total adsorbed protein and bound albumin content determine the loading capacity and release of dox payload. Protein densitometry reveals, that CTAB-SeNPs has the highest amount of bound albumin which in turn aided in enhanced loading of dox on the cationic NPs. The coronated-nanocarriers were further subjected to different pH-trigger, wherein all the coronated SeNPs had an enhanced dox release at pH- 4.6. The study also highlights that protein corona helps in impeding the burst release of dox from the conjugated system. Additionally, payload leakage study suggests, that bound corona proteins help in retaining dox and prevents significant desorption of the therapeutic molecule over time. However, the presence of positively charged dox disrupts the stability of the bound corona proteins making them prone to leakage. Finally, the cellular toxicity of the functionalized NPs were assessed, wherein dox-loaded protein coronated SeNPs induced significant cell death. The feasibility of employing protein-coronated-SeNPs as a new mode of drug delivery has been highlighted in this study.

Journal of Molecular Liquids

Utilizing corona on functionalized selenium nanoparticles for loading and release of doxorubicin payload

Selenium <a href="https://www.sciencedirect.com/topics/chemistry/nanoparticle">nanoparticles</a> paved its way into the field of medicine because of its lowered toxicity and excellent biological properties. Interaction between these nanoparticles and serum proteins leads to the formation of protein corona (hard and soft) on the nanoparticle surface modulating its biological behaviour and fate. In the present study, we have emphasized on the biocorona formation of most abundant serum proteins i.e. human serum albumin, immunoglobulin-G, and transferrin on functionalized selenium nanoparticles (CTAB, SDS, and brij-58). Changes in protein adsorption pattern, mean hydrodynamic size, and <a href="https://www.sciencedirect.com/topics/chemistry/zeta-potential">zeta potential</a> of differently functionalized selenium nanoparticles, following protein coronation were analysed for various incubation periods. Quantification of hard corona and soft corona for individual protein and for protein mixture was also done. The biological impact of protein coronation on selenium nanoparticles was evaluated by the cellular uptake and <a href="https://www.sciencedirect.com/topics/chemistry/cell-viability">cell viability</a> studies. Finally, modulation in radical scavenging property of selenium nanoparticles before and after protein corona formation was studied through DPPH assay.

Comprehensive study on biocorona formation on functionalized selenium nanoparticle and its biological implications

Gold nanorods (AuNRs) have distinctive opto-electronic properties, which facilitate their exploitation in various fields, especially biology and medicine. However, their interaction with the biomolecules in the physiological system can cause the formation of a protein corona, composing of a soft and hard layer, which ultimately alters the physiochemical properties, toxicity, and fate of the nanoparticles. Thus, the formation and composition of protein corona on three differently functionalized AuNRs [CTAB-AuNRs (positive), PEG-AuNRs (neutral), PSS-AuNRs (negative)] were studied for the three most abundant proteins in the blood serum namely, human serum albumin, immunoglobulin tG, and transferrin. The variation in protein adsorption, mean hydrodynamic size, and zeta potential were studied for different protein incubation periods (0, 0.5, 1, 4, 8, 12, and 24 h). The soft and hard corona layers were estimated for the individual proteins and mixture of the three proteins at the time point of maximum protein adsorption (1 h). Finally, in order to study the biological consequence of the coronation of AuNRs, the cell viability and uptake of AuNRs before and after protein corona formation were studied. The formation of IgG corona helped to reduce cellular toxicity, and at the same time, showed improved cell uptake when compared to the respective as-prepared AuNRs, highlighting their application potential for drug delivery applications. © 2017 Elsevier B.V.

Impact of gold nanorod functionalization on biocorona formation and their biological implication

Gold nanorods (AuNRs) used for biomedical applications could be encountered by biomolecules in the bloodstream, of which IgG is the most abundant antibody. With a view to mitigate their side effect on encountered proteins, the effect of Au concentration (5–40 μM) and functionalization (CTAB-positive;PSS-negative; PEG-neutral) of AuNRs was investigated on the stability of a model protein, IgG (1 μM). Electron microscopic images and particle size analyses indicated least aggregation behavior for PEG-AuNRs, which can be correlated to their neutral charge (from zeta potential analyses) or stearic hindrance of PEG chains. Variations in tryptophan domain were probed by UV–visible absorption and fluorescence quenching studies. Synchronous fluorescence study helped to provide information regarding variations in the hydrophobic region of IgG. The denaturation studies also indicated the stability of AuNR–IgG complex formation. These studies showed that positively charged IgG (pI: 7.8 ± 1.0) was mostly affected by negatively charged PSS-AuNRs and least affected by PEG-AuNRs. This was verified by secondary structural investigations performed using CD and FTIR spectroscopy. For cytotoxicity studies on human lymphocytes, CTAB-AuNRs are known to show higher toxicity compared to PSS-AuNRs and PEG-AuNRs (least). Though PSS-functionalized AuNRs were shown to affect cells to a lesser degree based on the negative charge of cell membrane, they could hamper with positively charged biomolecules in the bloodstream before they reach the target, which must also be considered for choosing the right AuNR functionalization. Thus, this work indicates the effect of different AuNR functionalization on protein and cellular toxicity and stresses the necessity to use neutral particles to mitigate their side effect for theranostic applications. © 2016 Elsevier B.V.

Materials Science and Engineering: C

Significance of surface functionalization of Gold Nanorods for reduced effect on IgG stability and minimization of cytotoxicity

Journal of King Saud University - Science

Novel development of nanoparticles to bimetallic nanoparticles and their composites: A review

Scientific Reports

Author Correction: Protein corona of airborne nanoscale PM2.5 induces aberrant proliferation of human lung fibroblasts based on a 3D organotypic culture

Journal	Data powered by TypesetBiomaterials Science
Publisher	Data powered by TypesetRoyal Society of Chemistry (RSC)
ISSN	2047-4830
Open Access	0