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Title: External architecture modification of ferritin molecules.
Authors: Lin, Agnes Huiling.
Keywords: DRNTU::Engineering::Chemical engineering::Biochemical engineering
Issue Date: 2009
Abstract: This project aims to expand the utilization of protein containers in nanotechnology. Ferritin is well-known to be an important molecule for iron storage. Since, it is a biological molecule, it can be further researched, on the ability of it to bind to nanoparticles and other metal ions. Ferritins are made up of 12 or 24 equal or not equal subunits. The typical ferritins are made up of 24 subunits, which is tetraeicosameric and they will fold into a 4-helical bundle. The ferritin shell is composed of both the H- subunit and the L- subunit which is the heavy and light chains respectively. Ferritins are found in both prokaryotes and eukaryotes and exist in highly conserved structure across the living organisms. The role of ferritin is to store and sequester iron in the hollow centre that allows for the binding of large amounts of iron in soluble, safe and bioavailable form. The iron will be released when they are required in the cell. Iron is an important element as it is required in cellular proliferation. The iron-sequestering capabilities of ferritin give it additional protection against oxidative stress which is involved in many diseases and disorders such as neurodegenerative diseases in humans. Ferritin iron can be extracted by numerous reducing agents and they are transported out of the shell via the hydrophilic channel on the 3-fold axes. In this project, ferritin will be developed to serve as a scaffold onto which nanomaterials, such as nanotubes, soft metals and drugs, can bind to. Specific non-interacting amino acids on the external architecture of the ferritin are modified using recombinant molecular biology techniques. Ferritins in this project are isolated from a hyperthermophilic marine Archaeon Archaeoglobus fulgidus.
Rights: Nanyang Technological University
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SCBE Student Reports (FYP/IA/PA/PI)

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