Date of Graduation
5-2016
Document Type
Thesis
Degree Name
Bachelor of Science in Chemical Engineering
Degree Level
Undergraduate
Department
Chemical Engineering
Advisor/Mentor
Servoss, Shannon
Committee Member/Reader
Hestekin, Jamie
Abstract
Amyloid beta protein has been linked to the formation of Alzheimer’s disease in patients.¹ Plaques form from amyloid beta fibrils. The formation of these plaques between neural connections in the brain are associated with Alzheimer’s disease.² The reduction of the formation of fibrils can be linked to utilizing protein mimics. The protocols that are used to reproduce the simulation of amyloid beta in the brain can be very important. Also, the structure of the protein mimic that is being used to inhibit the formation of fibrils can determine how the amyloid beta plaques are reduced.
The structure of sequence KLLFFLFFLLK peptoid was synthesized to test with amyloid beta. The amyloid beta must first be monomerized to the desired monomer 40 or 42 which are believed to be the main amino acid residues associated with the formation of plaques.³ This was accomplished through both 1,1,1,3,3,3 hexaprop-2-flouro treatment and fast protein liquid chromatography. The peptoid was synthesized by hand, purified by high pressure liquid chromatography, and tested by matrix-assisted laser desorption/ionization.
Citation
Motes, M. J. (2016). Investigating the Modulation of Aggregating Amyloid Beta 40. Chemical Engineering Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/cheguht/91