UMD Theses and Dissertations

Permanent URI for this collectionhttp://hdl.handle.net/1903/3

New submissions to the thesis/dissertation collections are added automatically as they are received from the Graduate School. Currently, the Graduate School deposits all theses and dissertations from a given semester after the official graduation date. This means that there may be up to a 4 month delay in the appearance of a given thesis/dissertation in DRUM.

More information is available at Theses and Dissertations at University of Maryland Libraries.

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Author: search.filters.author.Stock, Brian

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    Creating Localized Amyloid Nucleation of Silk-Elastin-Like Peptide Polymer Using Atomic Force Microscopy
    (2015) Stock, Brian; Seog, Joonil; Biophysics (BIPH); Digital Repository at the University of Maryland; University of Maryland (College Park, Md.)
    Research into amyloids was initially motivated by pathogenic amyloids involved in disease states such as Alzheimer's; however, new research implicates small oliogmeric species and not the mature fibers. This lack of toxicity has allowed for the development of amyloid-based biomaterials for use as nanowires, biosensors, and tissue regeneration. The directed self-assembly of peptides into amyloid-like fibers for use as biomaterials requires the ability to control both the nucleation location and growth direction of the fiber. We have used Atomic Force Microscopy to repeatedly stretch Silk-Elastin-Like Peptide Polymer (SELP) in the normal direction using continuous pulling in a force acquisition mode which has the ability to create nanodots of SELP at a specified location which are capable of nucleating SELP nanofibers. This work, if generalized to other amyloidogenic systems, may aid in the mechanistic understanding of the assembly process of both pathogenic and functional amyloids.