Name(s) of Faculty Adviser/Mentor

Dr. Michael R. Nichols

Document Type

Poster

Abstract

Alzheimer’s disease (AD) is characterized by chronic inflammation and neurodegeneration, which leads to loss of cognitive functions. Dr. Nichols’ research laboratory is studying the neurological effects associated with AD. Amyloid precursor protein (APP) is a membrane spanning protein whose primary function is unknown, but it is associated with many tissue types and found clustered at the synapse of neurons. APP can be cleaved by secretases into 40 or 42 amino acid fragments called amyloid beta protein (Aβ). These cleaved amyloid-β proteins can accumulate (aggregate) and form extracellular plaques in AD brains. Antibodies are normally produced in an adaptive immune response and are a high affinity binding protein that recognizes a specific molecule, whether it be a protein or foreign cellular component. Antibodies are commonly used in the lab to quantify the levels of aggregated proteins, such as Aβ and are often used in immunotherapy clinical trials to target plaques in AD patient’s brains. The aggregates of Aβ assemble into multiple different confirmations, some of which are soluble and others insoluble, but the most toxic and active form is the soluble protofibril form. Antibodies that have been made to be selective for the protofibril form of Aβ are required constantly to study the effect of Aβ. A combination of biological and biochemical techniques has been used to obtain the DNA sequence of a monoclonal antibody (mAbSL). The antibody mAbSL was purified with an affinity column and has been shown to be selective and specific for Aβ protofibrils by a series of immunological techniques, such as enzyme-linked immunosorbent assays (ELISA) and dot blots. With the sequence and means of expression we can create a stock of the antibodies and they will be applied in multiple aspects of this laboratory to help characterize Aβ protofibrils and their effects.

Publication Date

4-26-2019

Included in

Neurosciences Commons

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