News


Amyloidosis Foundation Awards 2015 Research Grants

The Amyloidosis Foundation awarded four research grants in December 2015. For the last ten years, the AF has funded promising clinical amyloidosis investigators from around the world. We applaud their efforts and look forward to the success this work will bring to patients.

 

H Landau 1Heather Landau, MD

Gene Expression Changes in AL amyloidosis

 

Amyloidosis Foundation – Donald C. Brockman Memorial Research Grant, 2015

 

Memorial Sloan Kettering Cancer Center, Medicine Division: Hematology

 

Amyloidosis is caused by the expansion of abnormal plasma cells that produce abnormal proteins that accumulate in tissues to cause end-organ damage.  To date, mutations in amyloid-forming plasma cells and their resulting consequences on the genes expressed have been poorly characterized.

This grant from the Amyloidosis Foundation will allow us to perform the first large-scale characterization of the mutations and gene expression changes in AL amyloidosis by evaluating patient’s plasma cells at diagnosis and following treatment. We expect such studies to allow us to identify genes that contribute to the development of disease, predict treatment responses, and identify new therapeutic targets. This study will play an important role in future development of a cure for amyloidosis.

 

MR picMichael Rosenzweig, MD

Cell Therapy for  AL amyloidosis

 

Amyloidosis Foundation – David Seldin, MD, PhD Memorial Research Grant, 2015

 

City of Hope, Medicine Division: Hematology & Hematopoietic Cell Transplantation

 

Amyloid light-chain (AL) amyloidosis is a rare blood disease that is treatable but often fatal. With the help of the Amyloidosis Foundation, we plan to develop a new treatment for AL amyloidosis by genetically engineering a patient’s own immune system to recognize and kill the abnormal blood cells when reintroduced into the body.

We will evaluate blood cells in patients with AL for expression of a specific protein that could be targeted by this approach. Once the target is identified, genetically engineered cells will be generated and tested in the laboratory. The ultimate goal is developing this therapy for clinical trials in patients with AL amyloidosis.

 

Lorena Saelices-AF-B&WLorena Saelices, PhD

New Strategy for TTR amyloidosis

 

 

 

Amyloidosis Foundation – Research Grant, 2015

 

Regents of the University of California

 

Treatments for systemic transthyretin amyloidosis have been held back by lack of information on the structures and causes of aggregation of the amyloid fibers formed by transthyretin (TTR). In previous work, we identified two protein segments involved in TTR aggregation, and developed a novel strategy to inhibit the process by small non-natural peptides.

Based on the amyloid structure of the aggregation-driving segments, we designed two peptide inhibitors that hindered TTR aggregation. With the support of the Amyloidosis Foundation in our research, these peptide inhibitors will be tested for their ability to halt fibril formation in the disease model of fruit flies. This new strategy will assist in providing successful therapies for TTR patients.

 

Towse B&WClare-Louise Towse, MChem, MPhil, PhD

Trying to Inhibit Amyloid Formation

 

Amyloidosis Foundation – Research Grant, 2015

 

University of Washington, Medicine Division: Office of Research

 

The proteins involved in amyloid diseases share an intermediate state that forms before the insoluble fibril form found in diseased tissue. This intermediate can be prevented from forming the fibrils by adding peptides, designed by the Daggett lab, in vitro. Our grant from the Amyloidosis Foundation will help us build on these designs by placing them inside a larger protein to increase their structural stability, which in turn is linked to their ability to prevent fibril formation.

We will be optimizing the designed peptides within the protein using computational methods and, once optimized, these molecules will be chemically synthesized and tested for the potential to inhibit amyloid formation. Results from this study will hopefully prevent amyloid formation in the future and give hope to amyloidosis patients.