Our interest focuses on a very unique state of protein — amyloid. Under certain conditions, proteins can self-assemble into amyloid aggregates, including oligomers and fibers. Amyloid aggregates formed by different proteins have long been related to >30 human devastating diseases, such as Alzheimer’s, Parkinson’s, type II diabetes, and cancer. In addition to pathogenic amyloids, more and more evidence show that a variety of amyloids, termed as “functional amyloid”, play important roles in many biological events including hormone storage and release, necroptosis which is a type of programmed cell death, and memory persistence. Many fundamental questions in the amyloid field remain unclear. For example, why certain kinds of amyloids are highly toxic while others are functional or beneficial to cells? What’s the structural basis of functional amyloid? What controls the transition between native state and amyloid state?

Our current main projects includes: 

1) Structural basis of pathological amyloid proteins aggregation including α-syn, Tau, FUS and hnRNPA1 which are key players in different neurodegenerative diseases (AD,PD and ALS); 

2) Method development for structural characterization of amyloids in vitro and in vivo (e.g. electron diffraction, in-cell NMR, IMMS); 

3) Molecular mechanism underlying the interplay between chaperones and amyloids; 

4) Structure-based design of inhibitor against pathological amyloid aggregation;

5) Structural studies of liquid-liquid phase separation of different proteins involved in important biological process and pathology; 

6) Design of amyloid biomaterials with applicable functions.