| Orlando,
Ron |
E-mail:
orlando@ccrc.uga.edu |
| My
research focuses on the use of mass spectrometry to answer biological
/ biomedical questions. The majority of our projects involve
characterizing the post-translational modifications (e.g., glycosylation,
phosphorylation) present in the protein of interest. For example,
we are currently investigating the in vivo changes that occur
in human eye lenses upon normal aging and cataract formation.
We hope that this research ultimately will provide a mechanism
to prevent cataracts. We also conduct research into developing
new methodologies to increase the amount of information obtained
from these MS experiments and to reduce the quantity of material
needed for analysis. |
| Keywords:
mass spectrometry, MS, characterization of post-translational
modifications, protein glycosylation, proteomics, protein identification,
liquid chromatography, LC/MS, matrix-assisted laser desorption
/ ionization MS, MALDI-MS, MS/MS |
|
| Przybyla,
Alan E. |
E-mail:
przybyla@bmb.uga.edu |
| One
hypothesis for the onset of Alzheimer's disease implicates small,
42 amino acid peptides known as Beta Amyloid peptides (AB42)
as the causative agents of the disease. Amyloid peptides arise
through proteolytic processing of a large, Type-1 membrane protein
precursor termed APP. The peptides are very hydrophobic and
after undergoing a structural conformational change to Beta
Sheets, they aggregate forming intercellular fibrils and plaques
in the cerebral cortex and hippocampus. The Alzheimic plaques
are toxic to neurons thus leading to the memory loss associated
with the disease. Using recombinantly expressed AB42 and mutant
peptides, our group is examining the kinetics and mechanisms
of fibril and plaques formation. As part of this process, we
generate 15N and 13C derivatives of the peptides to enhance
NMR studies aimed at determining the structure of native peptides,
conformationally altered peptides, and fibrils. Understanding
the peptide structure and the process of fibril formation will
lead to rational drug design focused at inhibiting the formation
of the plaques which are the causative agent of the disease. |
| Keywords:
Alzheimer's, Beta Amyloid, fibrilization, Amyloid oxidation,
scavenger receptors |
|
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