Molecularly Imprinted Nanogels Possessing Dansylamide Interaction Sites for Controlling Protein Corona In Situ by Cloaking Intrinsic Human Serum Albumin

Langmuir ◽  
2020 ◽  
Vol 36 (36) ◽  
pp. 10674-10682 ◽  
Author(s):  
Takahiro Morishita ◽  
Aoi Yoshida ◽  
Natsuki Hayakawa ◽  
Kentaro Kiguchi ◽  
Chehasan Cheubong ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Corona ◽  
Molecularly Imprinted ◽  
Interaction Sites

scholarly journals Development of In Situ Gelling Meloxicam-Human Serum Albumin Nanoparticle Formulation for Nose-to-Brain Application

Pharmaceutics ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 646
Author(s):  
Gábor Katona ◽  
Bence Sipos ◽  
Mária Budai-Szűcs ◽  
György Tibor Balogh ◽  
Szilvia Veszelka ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nasal Mucosa ◽  
Drug Absorption ◽  
Cell Damage ◽  
Lipid Fraction ◽  
Poloxamer 407 ◽  
Nasal Drug Delivery

The aim of this study was to develop an intranasal in situ thermo-gelling meloxicam-human serum albumin (MEL-HSA) nanoparticulate formulation applying poloxamer 407 (P407), which can be administered in liquid state into the nostril, and to increase the resistance of the formulation against mucociliary clearance by sol-gel transition on the nasal mucosa, as well as to improve drug absorption. Nanoparticle characterization showed that formulations containing 12–15% w/w P407 met the requirements of intranasal administration. The Z-average (in the range of 180–304 nm), the narrow polydispersity index (PdI, from 0.193 to 0.328), the zeta potential (between −9.4 and −7.0 mV) and the hypotonic osmolality (200–278 mOsmol/L) of MEL-HSA nanoparticles predict enhanced drug absorption through the nasal mucosa. Based on the rheological, muco-adhesion, drug release and permeability studies, the 14% w/w P407 containing formulation (MEL-HSA-P14%) was considered as the optimized formulation, which allows enhanced permeability of MEL through blood–brain barrier-specific lipid fraction. Cell line studies showed no cell damage after 1-h treatment with MEL-HSA-P14% on RPMI 2650 human endothelial cells’ moreover, enhanced permeation (four-fold) of MEL from MEL-HSA-P14% was observed in comparison to pure MEL. Overall, MEL-HSA-P14% can be promising for overcoming the challenges of nasal drug delivery.

Soft and Hard Interactions between Polystyrene Nanoplastics and Human Serum Albumin Protein Corona

2019 ◽  
Vol 30 (4) ◽  
pp. 1067-1076 ◽  
Author(s):  
Shinji Kihara ◽  
Nadine J. van der Heijden ◽  
Chris K. Seal ◽  
Jitendra P. Mata ◽  
Andrew E. Whitten ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Corona

scholarly journals Electrosynthesized molecularly imprinted polyscopoletin nanofilms for human serum albumin detection

2017 ◽  
Vol 977 ◽  
pp. 1-9 ◽  
Author(s):  
Zorica Stojanovic ◽  
Júlia Erdőssy ◽  
Katalin Keltai ◽  
Frieder W. Scheller ◽  
Róbert E. Gyurcsányi
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecularly Imprinted

scholarly journals A study on human serum albumin corona formed on photoluminescent carbon dots

2020 ◽  
Vol 44 (7-8) ◽  
pp. 447-452
Author(s):  
Peng Wang ◽  
Ming Yuan ◽  
Na Li ◽  
Feng Zhang
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Carbon Dots ◽  
Resonance Energy ◽  
Binding Constants ◽  
Protein Corona ◽  
Hybrid Nanomaterial ◽  
Corona Formation ◽  
Biomedical Field

Fluorescence nanostructures have been widely applied in the biomedical field as therapeutic agents and as novel tools for labeling, imaging, and sensing. However, the protein corona will dramatically influence the predesigned properties of nanostructures in serum. Therefore, it is important to understand the mechanism of protein corona formation on nanostructures. Photoluminescent carbon dots have been widely applied in the biomedical field since their discovery. Due to the large overlap between the absorption spectra of proteins and the fluorescence spectra of photoluminescent carbon dots, herein we investigate the mechanism of human serum albumin corona formed on photoluminescent carbon dots using fluorescence resonance energy transfer. By employing spectroscopic methods, the binding constants and the number of binding sites between human serum albumin and photoluminescent carbon dots have been determined, and the corresponding thermodynamics are also discussed as well for the interaction between photoluminescent carbon dots and human serum albumin. In addition, we successfully demonstrate the photoluminescent carbon dots in labeling bean sprouts. We believe that the current research cannot shed light on the mechanism of protein corona formation on nanostructures, but also could benefit the design of hybrid nanomaterial which will be applied to serum environments.

A durable antifouling protein molecularly imprinted gel interface for human serum albumin detection and antibacterial application

2021 ◽  
Vol 421 ◽  
pp. 129752
Author(s):  
Shuai Wang ◽  
Zhongmei Che ◽  
Chuanen Guo ◽  
Yinqi Liu ◽  
Shenghong Yang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecularly Imprinted

Human serum albumin stabilizes aqueous silver nanoparticle suspensions and inhibits particle uptake by cells

2018 ◽  
Vol 5 (4) ◽  
pp. 863-867 ◽  
Author(s):  
D. C. Kennedy ◽  
H. Qian ◽  
V. Gies ◽  
L. Yang
Keyword(s):  
Silver Nanoparticles ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Silver Nanoparticle ◽  
Protein Corona ◽  
Particle Uptake ◽  
Nanoparticle Suspensions ◽  
Commercial Polymers ◽  
Better Than

Human serum albumin forms a protein corona that stabilizes silver nanoparticles in water better than commercial polymers.

scholarly journals Are Zinc oxide nanoparticles safe? A structural study on human serum albumin using in vitro and in silico methods

2018 ◽  
Author(s):  
Marziyeh Hassanian ◽  
Hassan Aryapour ◽  
Alireza Goudarzi ◽  
Masoud Bezi Javan
Keyword(s):  
Zinc Oxide ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
In Silico ◽  
Zinc Oxide Nanoparticles ◽  
Protein Corona ◽  
Oxide Nanoparticles ◽  
Zno Nps

AbstractWith due attention to adsorption of proteins on the nanoparticles surface and the formation of nanoparticle-protein corona, investigation of nanoparticles toxicity on the structure of proteins is important. Therefore, this work was done to evaluate toxicity of Zinc oxide nanoparticles (ZnO NPs) on the structure of human serum albumin (HSA) through in vitro and in silico studies. First, ZnO NPs were synthesized using hydrothermal method and their size and morphology were determined by SEM and TEM methods and then to study its toxicity on the HSA structure were used UV-Vis and fluorescence spectroscopy. Also, in order to investigate interaction mechanism of ZnO NP with HSA at the atomistic level was used molecular dynamics (md) simulation. The obtained images from SEM and TEM showed that ZnO NPs were nanosheet with size of less than 40 nm. The results of spectroscopic studies showed ZnO NPs lead to significant conformational changes in the protein’s absorption and emission spectra. Moreover, md results showed the minor structure changes in HSA due to interaction with ZnO NP during the 100 ns simulation and the formation of nanoparticle-protein corona complex that is mainly because of electrostatic interactions between charge groups of HSA and ZnO NP.

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