Interaction of a Model Hydrophobic Drug Dimethylcurcumin with Albumin Nanoparticles

Das, Ram Pada; Singh, Beena G.; Kunwar, Amit; Priyadarsini, K. Indira

doi:10.1007/s10930-019-09866-z

Cited by 8 publications

(8 citation statements)

References 32 publications

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“…Mean hydrodynamic diameters ranging from 28 to 62 nm and corresponding zeta-potential values of −7.0 to −6.0 mV; increased cellular uptake and toxicity of DiMC A549 human lung cells Das et al (2017); Das et al (2019) Liposomes Thin-film hydration…”

Section: Dendrimer Thin Filmmentioning

confidence: 99%

“…Bovine serum albumin (BSA), which has ligand-binding properties and is widely available, cheap, and easily purified, is extensively used for drug delivery and well accepted in the pharmaceutical industry. In recent years, BSA nanoparticles have been used as an effective delivery system for hydrophobic drugs like DiMC ( Das et al, 2017 ; Das et al, 2019 ). Using the thermal denaturation method, BSA nanoparticles were prepared with mean hydrodynamic diameters ranging from 28 to 62 nm and corresponding zeta-potential values of −7.0 to −6.0 mV, which could easily bind DiMC to obtain drug-loaded nanoparticles.…”

Section: Nanoformulations Of Dimcmentioning

confidence: 99%

“…Using the A549 cell model, Das’s group further revealed such a kind of particle size effect that the cellular uptake and toxicity of DiMC increased with the increase in the particle size of these BSA-based nanoparticles ( Das et al, 2017 ). Their latest research demonstrated significant changes in the secondary structure of BSA upon particle formation and also a decrease in helicity ( Das et al, 2019 ). DiMC could be bound within the sub-domain IIA of BSA with a distance of about 24 Å between the hydrophobic core and the ligand, where it experienced a more rigid environment than in the native form of BSA.…”

Section: Nanoformulations Of Dimcmentioning

confidence: 99%

See 2 more Smart Citations

A Promising Anticancer Agent Dimethoxycurcumin: Aspects of Pharmacokinetics, Efficacy, Mechanism, and Nanoformulation for Drug Delivery

et al. 2021

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Curcumin is a well-known anticancer natural product with various significant bioactivities that has been well documented, but its widespread use is mainly hindered by insufficient ADME properties such as poor solubility and low metabolic stability. Dimethoxycurcumin (DiMC) is a kind of lipophilic compound derived from curcumin that maintains its anticancer potency and has greatly improved systematic bioavailability. Therefore, DiMC is regarded as a promising plant-derived anticancer agent that deserves to be well developed. Herein, we concentrate on the published work by those from original research groups concerned with the pharmacokinetics, efficacy, and mechanism of DiMC involved in the treatment of various tumors, as well as the nanoformulations for effective drug delivery.

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Section: Dendrimer Thin Filmmentioning

confidence: 99%

Section: Nanoformulations Of Dimcmentioning

confidence: 99%

Section: Nanoformulations Of Dimcmentioning

confidence: 99%

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A Promising Anticancer Agent Dimethoxycurcumin: Aspects of Pharmacokinetics, Efficacy, Mechanism, and Nanoformulation for Drug Delivery

et al. 2021

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“…24,25 Albumin NPs generally show a higher binding ability toward hydrophobic drugs than native albumin. 26 The affinity of a drug toward albumin is essential for its entrapment in NPs and delivery to its target sites. Recently, Li et al reported the interaction of BC with human serum albumin and bovine serum albumin (BSA), using fluorescence and Fourier transform infrared spectroscopy techniques, in which hydrophobic forces and electrostatic attraction play a significant role.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and characterization of β‐carotene‐loaded albumin nanoparticles by high‐speed homogenizer

Yang

Park³

et al. 2022

Bulletin Korean Chem Soc

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β‐Carotene (BC) is a strong antioxidant, but its therapeutic application has been limited by its poor aqueous solubility. Protein‐based nanoparticles (NPs) have been used to increase the aqueous solubility of hydrophobic drugs. In this study, bovine serum albumin (BSA) was used to prepare NPs to encapsulate BC using a high‐speed homogenizer. After homogenization, BC‐BSA‐NPs were formed and the encapsulated BC was dissolved in phosphate‐buffered saline at pH 7.4. Various characterization methods, including dynamic light scattering, transmission electron microscopy, and spectrophotometry, indicated that BC‐BSA‐NPs were spherical with an average size of 112 nm and encapsulated BC with high efficiency. BC encapsulated in NPs was stable during the preparation process and was continuously released in PBS at 37 °C for 3 days. The 2,2‐diphenyl‐1‐picrylhydrazyl and ferric reducing antioxidant power assays demonstrated good antioxidant activity of BC‐BSA‐NPs. These results suggest that BSA‐NPs are a promising nanocarrier for the delivery of BC.

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“…A strong structure–function correlation governs the functionality of proteins as their biological activity is guaranteed only when they obtain a three‐dimensional (3D) native conformation through folding pathway 1 . However, structure rearrangement of proteins is readily occurred on interaction with exogenous agents like surfactants, ions, nanoparticles (NPs), and so on 2‐7 . Recently, many research studies have been allocated to the challenges facing the interaction of proteins with NPs as the application of NPs in biological systems has gained much attention.…”

Section: Introductionmentioning

confidence: 99%

Promising insights into the kosmotropic effect of magnetic nanoparticles on proteins: The pivotal role of protein corona formation

Fattah

Rashedi

Yazdian

et al. 2020

Biotechnology Progress

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Increasing concerns about biosafety of nanoparticles (NPs) has raised the need for detailed knowledge of NP interactions with biological molecules especially proteins. Herein, the concentration-dependent effect of magnetic NPs (MNPs) on bovine serum albumin and hen egg white lysozyme was explored. The X-ray diffraction patterns, zeta potential, and dynamic light scattering measurements together with scanning electron microscopy images were employed to characterize MNPs synthesized through coprecipitation method. Then, we studied the behavior of two model proteins with different surface charges and structural properties on interaction with Fe 3 O 4. A thorough investigation of protein-MNP interaction by the help of intrinsic fluorescence at different experimental conditions revealed that affinity of proteins for MNPs is strongly affected by the similarity of protein and MNP surface charges. MNPs exerted structure-making kosmotropic effect on both proteins under a concentration threshold; however, binding strength was found to determine the extent of stabilizing effect as well as magnitude of the concentration threshold. Circular dichroism spectra showed that proteins with less resistance to conformational deformations are more prone to secondary structure changes upon adsorption on MNPs. By screening thermal aggregation of proteins in the presence of Fe 3 O 4 , it was also found that like chemical stability, thermal stability is influenced to a higher extent in more strongly bound proteins. Overall, this report not only provides an integrated picture of protein-MNP interaction but also sheds light on the molecular mechanism underling this process.

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Interaction of a Model Hydrophobic Drug Dimethylcurcumin with Albumin Nanoparticles

Cited by 8 publications

References 32 publications

A Promising Anticancer Agent Dimethoxycurcumin: Aspects of Pharmacokinetics, Efficacy, Mechanism, and Nanoformulation for Drug Delivery

A Promising Anticancer Agent Dimethoxycurcumin: Aspects of Pharmacokinetics, Efficacy, Mechanism, and Nanoformulation for Drug Delivery

Synthesis and characterization of β‐carotene‐loaded albumin nanoparticles by high‐speed homogenizer

Promising insights into the kosmotropic effect of magnetic nanoparticles on proteins: The pivotal role of protein corona formation

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