Current Search: Wojcikiewicz, Ewa P. (x)
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Title
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Investigation of cell stiffness and cytoskeletal remodeling in response to inflammatory mediators using atomic force microscopy (AFM).
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Creator
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Magny, Sherlyne, Wojcikiewicz, Ewa P.
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Date Issued
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2013-04-05
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PURL
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http://purl.flvc.org/fcla/dt/3361120
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Subject Headings
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Atomic force microscopy, Inflammation--Mediators, Cancer cells, Cytoskeleton
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Format
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Document (PDF)
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Title
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Characterizing the Biophysical Mechanism of Cell-penetrating Peptides in Cancer Cell Entry.
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Creator
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Mary Moussa, Shalondria Sears, Patrick Cosme, Andrew C. Terrentis, Ewa P. Wojcikiewicz
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Date Issued
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2017
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PURL
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http://purl.flvc.org/fau/fd/FAU_SR00000017
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Subject Headings
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College students --Research --United States.
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Format
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Document (PDF)
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Title
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Effect of PAK6 Knowckout on Prostate Cancer Cell Stiffness.
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Creator
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Nikolas B. Echeverry, Belinda Gerard, Michael L. Lu, Ewa P. Wojcikiewicz
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Date Issued
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2017
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PURL
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http://purl.flvc.org/fau/fd/FAU_SR00000008
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Subject Headings
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College students --Research --United States.
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Format
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Document (PDF)
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Title
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Gold Nanoparticles as a Probe for Amyloid-β Oligomer and Amyloid Formation.
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Creator
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Esmail A. Elbassal, Clifford Morris, Thomas W. Kent, Thomas W. Kent, Bimlesh Ojha, Ewa P. Wojcikiewicz, Deguo Du
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Abstract/Description
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The process of amyloid-β (Aβ) amyloid formation is pathologically linked to Alzheimer’s disease (AD). The identification of Aβ amyloids and intermediates that are crucial players in the pathology of AD is critical for exploring the underlying mechanism of Aβ aggregation and the diagnosis of the disease. Herein, we performed a gold nanoparticle (AuNP)-based study to detect the formation of Aβ amyloid fibrils and oligomers. Our results demonstrate that the intensity of the surface plasmon...
Show moreThe process of amyloid-β (Aβ) amyloid formation is pathologically linked to Alzheimer’s disease (AD). The identification of Aβ amyloids and intermediates that are crucial players in the pathology of AD is critical for exploring the underlying mechanism of Aβ aggregation and the diagnosis of the disease. Herein, we performed a gold nanoparticle (AuNP)-based study to detect the formation of Aβ amyloid fibrils and oligomers. Our results demonstrate that the intensity of the surface plasmon resonance (SPR) absorption band of the AuNPs is sensitive to the quantity of Aβ40 amyloids. This allows the SPR assay to be used for detection and semi-quantification of Aβ40 amyloids, and characterization of the kinetics of Aβ amyloid formation. Furthermore, our study demonstrates that the SPR band intensity of the AuNPs is sensitive to the presence of oligomers of both Aβ40 and an Aβ40 mutant, which forms more stable oligomers. The kinetics of the stable oligomer formation of the Aβ40 mutant can also be monitored following the SPR band intensity change of AuNPs. Our results indicate that this nanoparticle based method can be used for mechanistic studies of early protein self-assembly and fibrillogenesis.
Show less
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Date Issued
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2017
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PURL
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http://purl.flvc.org/fau/fd/FAUIR000499
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Format
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Document (PDF)
