Researchers at Rensselaer Polytechnic Institute Develop Antibodies With Improved Ability for Preventing Formation of Toxic Protein Particles Linked to Diseases Including Alzheimer’s and Parkinson’s
Antibodies developed by researchers at Rensselaer Polytechnic Institute are unusually effective at preventing the formation of toxic protein particles linked to Alzheimer’s disease and Parkinson’s disease, as well as Type 2 diabetes, according to a new study.
The onset of these devastating diseases is associated with the inappropriate clumping of proteins into particles that are harmful to cells in the brain (Alzheimer’s disease and Parkinson’s disease) and pancreas (Type 2 diabetes). Antibodies, which are commonly used by the immune system to target foreign invaders such as bacteria and viruses, are promising weapons for preventing the formation of toxic protein particles. A limitation of conventional antibodies, however, is that high concentrations are required to completely inhibit the formation of toxic protein particles in Alzheimer’s, Parkinson’s, and other disorders.
To address this limitation, a team of researchers led by Rensselaer Professor Peter Tessier has developed a new process for creating antibodies that potently inhibit formation of toxic protein particles. Conventional antibodies typically bind to one or two target proteins per antibody. Antibodies created using Tessier’s method, however, bind to 10 proteins per antibody. The increased potency enables the novel antibodies to prevent the formation of toxic protein particles at unusually low concentrations. This is an important step toward creating new therapeutic molecules for preventing diseases such as Alzheimer’s and Parkinson’s.
“It is extremely difficult to get antibodies into the brain. Less than 5 percent of an injection of antibodies into a patient’s blood stream will enter the brain. Therefore, we need to make antibodies as potent as possible so the small fraction that does enter the brain will completely prevent formation of toxic protein particles linked to Alzheimer’s and Parkinson’s disease,” said Tessier, assistant professor in the Howard P. Isermann Department of Chemical and Biological Engineering at Rensselaer. “Our strategy for designing antibody inhibitors exploits the same molecular interactions that cause toxic particle formation, and the resulting antibodies are more potent inhibitors than antibodies generated by the immune system.”
Results of the new study, titled “Rational design of potent domain antibody inhibitors of amyloid fibril assembly,” were published online last week by the journal Proceedings of the National Academy of Sciences (PNAS). The study may be viewed at: http://www.pnas.org/content/early/2012/11/14/1208797109.abstract
This research was conducted in the laboratories of the Center for Biotechnology and Interdisciplinary Studies at Rensselaer.
Tessier’s research represents a new way of generating therapeutic antibodies. Currently, most antibodies are obtained by exploiting the immune system of rodents. Mice are injected with a target protein, for example the Alzheimer’s protein, and the animal’s immune system generates an antibody specific for the target protein. Tessier’s method is radically different as it relies on rational design approaches to create antibodies based on properties of the target proteins.
Along with Tessier, co-authors of the paper are Rensselaer graduate students Ali Reza Ladiwala, Moumita Bhattacharya, Joseph Perchiaccaa; Ping Cao and Daniel Raleigh of the Department of Chemistry at Stony Brook University; Andisheh Abedini and Ann Marie Schmidt of the Diabetes Research Program at New York University School of Medicine; and Jobin Varkey and Ralf Langen of the Zilkha Neurogenetic Institute at the University of Southern California, Los Angeles.
This study was funded with support from the American Health Assistance Foundation, the National Science Foundation, the Pew Charitable Trust, and the National Institutes of Health.
For more information on Tessier and his research at Rensselaer, visit:• Tessier Lab Website
Michael Mullaney | Newswise
‘Farming’ bacteria to boost growth in the oceans
24.10.2016 | Max-Planck-Institut für marine Mikrobiologie
Calcium Induces Chronic Lung Infections
24.10.2016 | Universität Basel
Terahertz excitation of selected crystal vibrations leads to an effective magnetic field that drives coherent spin motion
Controlling functional properties by light is one of the grand goals in modern condensed matter physics and materials science. A new study now demonstrates how...
Researchers from the Institute for Quantum Computing (IQC) at the University of Waterloo led the development of a new extensible wiring technique capable of controlling superconducting quantum bits, representing a significant step towards to the realization of a scalable quantum computer.
"The quantum socket is a wiring method that uses three-dimensional wires based on spring-loaded pins to address individual qubits," said Jeremy Béjanin, a PhD...
In a paper in Scientific Reports, a research team at Worcester Polytechnic Institute describes a novel light-activated phenomenon that could become the basis for applications as diverse as microscopic robotic grippers and more efficient solar cells.
A research team at Worcester Polytechnic Institute (WPI) has developed a revolutionary, light-activated semiconductor nanocomposite material that can be used...
By forcefully embedding two silicon atoms in a diamond matrix, Sandia researchers have demonstrated for the first time on a single chip all the components needed to create a quantum bridge to link quantum computers together.
"People have already built small quantum computers," says Sandia researcher Ryan Camacho. "Maybe the first useful one won't be a single giant quantum computer...
COMPAMED has become the leading international marketplace for suppliers of medical manufacturing. The trade fair, which takes place every November and is co-located to MEDICA in Dusseldorf, has been steadily growing over the past years and shows that medical technology remains a rapidly growing market.
In 2016, the joint pavilion by the IVAM Microtechnology Network, the Product Market “High-tech for Medical Devices”, will be located in Hall 8a again and will...
14.10.2016 | Event News
14.10.2016 | Event News
12.10.2016 | Event News
24.10.2016 | Earth Sciences
24.10.2016 | Life Sciences
24.10.2016 | Physics and Astronomy