Tag: amyloid
How does a curved molecule fit into a flat binding pocket? Structural basis for the stabilization of amyloidogenic immunoglobulin light chains by hydantoins. Nicholas L. Yan, Diogo Santos-Martins, Enrico Rennella, Brittany B. Sanchez, Jason S. Chen, Lewis E. Kay, Ian A. Wilson, Gareth J. Morgan, Stefano Forli, Jeffery W. Kelly Bioorganic & Medicinal Chemistry Letters […]
We have developed a new method for measuring protein stability that can be used in high throughput screens. We hope that this will be a useful alternative to existing methods for researchers looking for molecules that bind to and stabilize proteins. Details are in our new paper. Proteins are dynamic, flexible polymers that can form […]
A major goal of the lab is to develop new therapies for amyloidosis. Today, our paper describing a big step towards a drug for AL amyloidosis was published. We have identified small molecules that bind to antibody light chains and prevent them from unfolding, which could potentially reduce amyloid formation in patients. We’re a long […]
Two manuscripts were published last week describing high-resolution 3D structures of light chain amyloid fibrils extracted from patient heart tissue. Swuec and coworkers solved the structure of a fibril derived from a lambda 6-57 light chain using cryo electron microscopy (cryoEM); Radameker and coworkers did the same for a lambda 1-44 light chain. These structures […]