Lantz, Carter
Carter is in the Biochemistry, Molecular and Structural Biology Graduate Program, and joined the CMB training program in 2018. He received a B.A. degree in Biochemistry and Mathematics from Baylor University.
Mentor: Dr. Joseph Loo
Many neurodegenerative diseases have been found to involve the formation of aggregated proteins in the brain. Among these diseases are Alzheimer’s disease, characterized by plaques of amyloid beta and neurofibrillary tangles of tau, and Parkinson’s disease, with Lewy bodies of α-synuclein as its hallmark. These aggregates cause the death of neurons and lead to symptoms common in Alzheimer’s and Parkinson’s patients. Although extensive research has focused on these proteins, the mechanism of fibril formation is still a mystery.
My project utilizes mass spectrometry (MS) and electron microscopy (EM) to determine how post-translational modifications and aggregation inhibiting compounds affect amyloid protein structure. Phosphorylation of amyloid proteins has been linked to the development of protein fibrils in neurons. MS analysis may show changes in protein structure due to phosphorylation; EM of these fibrils may show differences in fibril morphology due to phosphorylation. In addition, many compounds have been shown to inhibit the aggregation of amyloid proteins. MS analysis will determine the location and structural implications of compound binding. These analyses will hopefully bring insight into the role of protein aggregation in neurodegenerative diseases and help forward possible treatments for these diseases.
