Title

Knob Socket Analysis of Beta Amyloid Proteins

Poster Number

30

Lead Author Major

Pre-Dentistry

Format

Poster Presentation

Faculty Mentor Name

Jerry Tsai

Faculty Mentor Department

Chemistry

Additional Faculty Mentor Name

Hyun Joo

Abstract/Artist Statement

Alzheimer's disease is an irreversible brain disorder that gradually destroys memory, critical thinking skills, and the ability to carry out simple tasks. Currently, this disease affects 5.2 million Americans. Alzheimer's has been characterized by the formation of beta-amyloid peptide plaques between nerve cells in the brain. Analysis of the three-dimensional tertiary protein structure is a challenge, but could result in better development of therapeutic and diagnostic tests. The knobsocket model simplifies the complexity of threedimensional packing of protein residues into an easily interpretable two-dimensional map. The resulting topology map of tertiary structure clearly indicates how the amino acid residues interact with each other as a group and individually. The local set of amino acid residues form a three member socket, while a non-local residue is defined as the knob that packs into the socket. The Alzheimer disease state has been shown to be caused by prion amyloids, and structural information about these amyloids have been solved for the protein crystals 2LMN and 2LMP. Using the knob-socket model, packing topology maps were constructed for these amyloid states. These topology maps identify potential areas on the exposed amyloid surface that could interaction with a diagnostic peptide to identify early stages of the disease. Also, the exposed edges offer areas of interaction to inhibit further extension of the prion state and therefore a potential therapeutic by preventing amyloid plaque growth. The next steps are to synthesize these peptides that target the amyloid structure and test their binding ability and inhibition of amyloid plaque accumulation.

Location

DeRosa University Center, Ballroom

Start Date

30-4-2016 1:30 AM

End Date

30-4-2016 3:30 PM

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Apr 30th, 1:30 AM Apr 30th, 3:30 PM

Knob Socket Analysis of Beta Amyloid Proteins

DeRosa University Center, Ballroom

Alzheimer's disease is an irreversible brain disorder that gradually destroys memory, critical thinking skills, and the ability to carry out simple tasks. Currently, this disease affects 5.2 million Americans. Alzheimer's has been characterized by the formation of beta-amyloid peptide plaques between nerve cells in the brain. Analysis of the three-dimensional tertiary protein structure is a challenge, but could result in better development of therapeutic and diagnostic tests. The knobsocket model simplifies the complexity of threedimensional packing of protein residues into an easily interpretable two-dimensional map. The resulting topology map of tertiary structure clearly indicates how the amino acid residues interact with each other as a group and individually. The local set of amino acid residues form a three member socket, while a non-local residue is defined as the knob that packs into the socket. The Alzheimer disease state has been shown to be caused by prion amyloids, and structural information about these amyloids have been solved for the protein crystals 2LMN and 2LMP. Using the knob-socket model, packing topology maps were constructed for these amyloid states. These topology maps identify potential areas on the exposed amyloid surface that could interaction with a diagnostic peptide to identify early stages of the disease. Also, the exposed edges offer areas of interaction to inhibit further extension of the prion state and therefore a potential therapeutic by preventing amyloid plaque growth. The next steps are to synthesize these peptides that target the amyloid structure and test their binding ability and inhibition of amyloid plaque accumulation.