Under many aqueous conditions, metal oxide nanoparticles attract other nanoparticles and grow into fractal aggregates as the result of a balance between electrostatic and Van Der Waals interactions. Although particle coagulation has been studied for over a century, the effect of light on the state of aggregation is not well understood. Since nanoparticle mobility and toxicity have been shown to be a function of aggregate size, and generally increase as size decreases, photo-induced disaggregation may have significant effects. We show that ambient light and other light sources can partially disaggregate nanoparticles from the aggregates and increase the dermal transport of nanoparticles, such that small nanoparticle clusters can readily diffuse into and through the dermal profile, likely via the interstitial spaces. The discovery of photoinduced disaggregation presents a new phenomenon that has not been previously reported or considered in coagulation theory or transdermal toxicological paradigms. Our results show that after just a few minutes of light, the hydrodynamic diameter of TiO(2) aggregates is reduced from ∼280 nm to ∼230 nm. We exposed pigskin to the nanoparticle suspension and found 200 mg kg(-1) of TiO(2) for skin that was exposed to nanoparticles in the presence of natural sunlight and only 75 mg kg(-1) for skin exposed to dark conditions, indicating the influence of light on NP penetration. These results suggest that photoinduced disaggregation may have important health implications.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3498245 | PMC |
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0048719 | PLOS |
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December 2024
Department of Basic Medical Sciences, College of Veterinary Medicine, Purdue University, West Lafayette, IN 47907, United States. Electronic address:
Tau and α-synuclein (α-syn) are prone-to-aggregate proteins that can be responsible for pathological lesions found in the brains of Alzheimer's disease (AD), Lewy body dementia (LBD), and Parkinson's disease (PD) patients. The early-stage oligomers and protofibrils of tau are believed to be strongly linked to human cognitive impairment while the toxic α-syn oligomers are associated with behavioral motor deficits. Therefore, concurrent targeting of both proteinaceous aggregates and oligomers are very challenging.
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November 2024
Department of Basic Medical Sciences, College of Veterinary Medicine, Purdue University, West Lafayette, Indiana 47907, United States.
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January 2024
Institute of Physiologically Active Compounds at Federal Research Center of Problems of Chemical Physics and Medicinal Chemistry, Russian Academy of Sciences (IPAC RAS), Chernogolovka, Russia.
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View Article and Find Full Text PDFACS Chem Neurosci
November 2023
Department of Basic Medical Sciences, College of Veterinary Medicine, Purdue University, West Lafayette, Indiana 47907, United States.
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View Article and Find Full Text PDFInt J Biol Macromol
June 2023
Department of Chemistry, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi'an 710072, PR China. Electronic address:
Photoinduced modulation of Aβ aggregation has emerged as a therapeutic option for treating Alzheimer's disease (AD) due to its high spatiotemporal controllability, noninvasive nature, and low systemic toxicity. However, existing photo-oxidants have the poor affinity for Aβ, low depolymerization efficiency, and difficulty in crossing the blood-brain barrier (BBB), hindering their application in the treatment of AD. Here, through hydrophobic interactions and hydrogen bonding, we integrated the near-infrared (NIR) photosensitizer indocyanine green with transferrin (denoted as TF-ICG), a protein with a high affinity for Aβ, and demonstrated its anti-amyloid activity in vitro.
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