Unlike “globular” proteins that adopt stable structures that are relatively easy to analyze, intrinsically disordered proteins adopt many context-dependent shapes. These shapes may drive diverse functions, but they are also difficult to capture and study. This represents a large gap in our understanding of biology, given that most proteins may have intrinsically disordered regions. Thankfully, researchers like Professor Priyanka Joshi, Ph.D., from Georgetown University have devoted themselves to studying intrinsically disordered proteins and are developing new approaches and leveraging new technologies like the Nautilus Voyager™ Platform to discover how their dynamic structures influence biological function. Because intrinsically disordered proteins often aggregate in disease, this work is not only essential to our understanding of biology but may also enable the development of effective biomarkers and treatments for diseases like Alzheimer’s.
Parag interviews Professor Joshi on this episode of Translating Proteomics to discover:
00:00 – Introduction to Prof. Priyanka Joshi, Ph.D.
04:35 – What are intrinsically disordered proteins (IDPs)?
11:41 – When do intrinsically disordered proteins go bad in disease?
23:02 – Archetypal Intrinsically disordered proteins – c-Myc/Max, p53, and Tau
38:26 – Barriers to solving the problems associated with intrinsically disordered proteins
43:30 – The future of intrinsically disordered protein research and introducing the SEEDS Consortium
Additional resources featured in the episode:https://pubmed.ncbi.nlm.nih.gov/26923286/
Joshi, Priyanka et al. “A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.” ACS combinatorial science vol. 18,3 (2016): 144-53. doi:10.1021/acscombsci.5b00129
Priyanka’s 2016 work developing small-molecule libraries to target IDPs
Georgetown University press release covering the SEEDS Consortium
Nautilus Biotechnology press release covering its involvement in the SEEDS Consortium
