Our
lab focuses on understanding the mechanisms of protein misfolding and
aggregation in degenerative diseases. Alzheimer's disease (AD),
Parkinson's disease (PD), dementia with Lewy bodies (DLB), progressive
supranuclear palsy (PSP), macular degeneration, Type II diabetes,
Huntington's disease, prion diseases, and serum amyloidoses are only a
few of the conditions that result from amyloid and tau oligomer
misfolding and aggregation. As this list grows, it becomes vital to
understand the mechanisms of amyloid formation, accumulation, and
protein assembly. Soluble oligomers and protofibrils are significant in
the pathogenesis of these diseases. These species are not only common
among all amyloidogenic proteins, but they also share common structural
features regardless of their sequence.
An emerging view in
neurodegeneration is that the large meta-stable tau aggregates such as,
plaques and neurofibrillary tangles (NFT) are not toxic; rather, it is
the intermediate amyloid and tau aggregates (oligomers) that are
pathogenic. One of the many approaches we use is to exploit our
knowledge of amyloid and tau oligomer structure to prepare novel
antigens that elicit a specific immune response. This approach allows us
to avoid unwanted autoimmune responses or interference with folded,
functional proteins. This concept of generating conformation-specific
antibodies not only makes it possible to study these diseases in vivo,
but it may enable us to develop a safe therapeutic vaccine to prevent
or treat these devastating diseases. Our lab also screens commercially
available and novel drug-like small-molecules to identify inhibitors of
oligomer formation.
We are also
interested in studying pore-forming toxins, bacterial amyloid and
biofilm. We are using our novel antibodies to prevent toxin-induced
hemolysis and neutralize bacterial amyloid's infectious properties and
prevent human diseases.
Search PubMed for Dr. Kayed's publications