On Thursday, November 3, the Rensselaer Center for Biotechnology and Interdisciplinary Studies had its second Public Interest Forum. The topic of this forum was “Understanding Alzheimer’s Disease.” The Director of Biotech, Jonathan Dordick, announced the purpose of these forums was to inform and inspire professors of other disciplines, undergraduates, and curious learners both in and out of the institution to some critical topics being worked on at the Biotech center presently. Dordick asserted, “Research at the Biotech [is] helping to move from randomness to something more concrete. He then briefly introduced the three speakers: Chunyu Wang, Wilfredo Colon, and Peter Tessier and told the audience that the talks today will help explain Alzheimer’s disease on the molecular or protein level. After all, the cause of many diseases is the result of proteins that act abnormally, causing neural function to decrease.
The first speaker was Associate Professor of Biology Chunyu Wang with a presentation entitled “The Mechanism and Drug Discover in Alzheimer’s Disease.” He started his presentation by stating that 35 million people are diagnosed with the disease, of which five million are Americans. It costs roughly 600 billion dollars for their collective treatment. He then progressed to talk about the studies of the structural mechanism of AD using nuclear magnetic resonance, molecular dynamics simulations, biochemistry, and biophysics. His specific research focused on the structural mechanism of Amyloid beta, which is a peptide of 36–43 amino acids processed from the Amyloid precursor protein known to be associated with both types of AD. The disease can be either sporadic or familial and is caused by mutations.
Wang focused specifically on Abeta40 and Abeta42, “the yin and yang of AD.” While these peptides might only vary by two amino acids, their structural components are far different. Wang realized that a patient with AD had an increased ratio of Abeta42 to Abeta40, leading to the prediction that aggregation of Abeta42 causes increased familial AD and that Abeta40 may eventually prevent and cure AD. Wang wanted to further tackle how the structure of Abeta42 is related to toxicity and memory loss. Using silicon screening, both structures have been mapped out. Wang then knew that Abeta and Cyclophilin D join together cause harmful molecules to leak out in a process called mitochondrial dysfunction. Hence he is currently leading projects on how Abeta and Cyclophilin D interact. Only four drugs are currently on the market based on acetylcholine receptor. With Wang’s research perhaps more can be put out.
The second speaker was the Associate Professor of Chemistry and general chemistry lecturer, Wilfredo (Freddie) Colon. His presentation was entitled “Alzheimer’s Disease: Why does Abeta accumulate?” Colon believes that the disease needs to be delayed, not cured, and wants to know why Abeta accumulates, as scientists do not know what triggers accumulation in 95 percent of AD. Colon believes that the protein degradation machinery is compromised, causing Abeta toxic species to be difficult to degrade. Some factors that might comprise our protein degradation system include aging, genetic factors, external factors such as damage caused by exposure or inflation, overproduction of Abeta, and deficiencies in the metabolism.
However, some toxic Abeta species may be resistant to degradation due to kinetic stability—it has to do with being trapped. Abnormal loss or gain of kinetic stability can result in AD, Parkinson’s disease, or even Mad Cow disease. Colon hypothesized that the toxic Abeta species that are kinetically stable might play a pathological role in AD and wanted to discover and implement a biomarker approach.
The last speaker, Peter Tessier, is an assistant professor of Chemical and Biological Engineering. Tessier reviewed some of the general concepts of AD, describing it as one of the greatest challenges of our time and how a neuron with Amyloid plague results in AD. His research focused on how the proteins were packed, and how different packing arrangements result in either benign formations or toxic formations. He is currently working on changing the shapes or disassociating the proteins that aggregate back to monomers.
After the three speakers was a panel discussion where the audience had the opportunity to ask questions they had after listening to the three talks. The event was considered a success by Dordick, as so many people of the audience participated. After the panel discussion a reception was held with hors d’oeuvres and refreshments.