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Chemical Engineering

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The University of Akron

2011

Articles 1 - 2 of 2

Full-Text Articles in Engineering

Polymorphic Structures Of Alzheimer's Beta-Amyloid Globulomers, Jie Zheng Oct 2011

Polymorphic Structures Of Alzheimer's Beta-Amyloid Globulomers, Jie Zheng

Chemical, Biomolecular, and Corrosion Engineering Faculty Research

Misfolding and self-assembly of Amyloid-β (Aβ) peptides into amyloid fibrils is pathologically linked to the development of Alzheimer's disease. Polymorphic Aβ structures derived from monomers to intermediate oligomers, protofilaments, and mature fibrils have been often observed in solution. Some aggregates are on-pathway species to amyloid fibrils, while the others are off-pathway species that do not evolve into amyloid fibrils. Both on-pathway and off-pathway species could be biologically relevant species. But, the lack of atomic-level structural information for these Aβ species leads to the difficulty in the understanding of their biological roles in amyloid toxicity and amyloid formation.


Hemocompatibility Of Silicon-Based Substrates For Biomedical Implant Applications, Lingyan Liu Apr 2011

Hemocompatibility Of Silicon-Based Substrates For Biomedical Implant Applications, Lingyan Liu

Chemical, Biomolecular, and Corrosion Engineering Faculty Research

Silicon membranes with highly uniform nanopore sizes fabricated using microelectromechanical systems (MEMS) technology allow for the development of miniaturized implants such as those needed for renal replacement therapies. However, the blood compatibility of silicon has thus far been an unresolved issue in the use of these substrates in implantable biomedical devices. We report the results of hemocompatibility studies using bare silicon, polysilicon, and modified silicon substrates. The surface modifications tested have been shown to reduce protein and/or platelet adhesion, thus potentially improving biocompatibility of silicon. Hemocompatibility was evaluated under four categories—coagulation (thrombin–antithrombin complex, TAT generation), complement activation (complement protein, C3a …