Sunil Kumar, PhD
Name of Institution:
University of Denver, Denver, CO
Therapeutic validation of novel targets associated with Parkinson’s disease
Dr. Kumar received his PhD at Clemson University in South Carolina, where the focus of his research was the design and synthesis of novel aminoglycosides to target various forms of nucleic acids. He did postdoctoral fellowships in the labs of Dr. Andrew D. Miranker at Yale University in Connecticut and Dr. Andrew D. Hamilton at New York University. In his postdoctoral training, he utilized synthetic protein mimetic-based approaches to investigate the structure and function of various amyloid proteins. He is currently an Assistant Professor in the Department of Chemistry and Biochemistry and the Knoebel Institute for Healthy Aging at The University of Denver. The central theme of his lab is the design of tools – synthetic, biophysical, and in vivo – to gain mechanistic and therapeutic insights into various diseases, including Parkinson’s disease (PD).
To identify drug-like ligands that can specifically target and disrupt the aggregation of α-synuclein, a process that is directly associated with development of PD.
The pathological hallmark of PD involves the aggregation of functional α-synuclein into non-functional amyloid structures. One of the potential therapeutic interventions against PD is the effective inhibition of α-synuclein aggregation.
We will use a biochemical approach in tandem with numerous in vitro and in vivo PD models to identify ligands that can specifically target α-synuclein sequences, which mediate the formation of neurotoxic α-synuclein oligomers/fibers. We aim to mimic the chemical and structural fingerprints of the α-synuclein protein surface during the aggregation of α-synuclein in order to block the aggregation process.
Relevance to Diagnosis/Treatment of Parkinson’s Disease:
This proposed study seeks to identify novel potential therapeutics that disrupt the process of α-synuclein aggregation, a process central to the development of PD. We envision that the identification of molecules that disrupt the aggregation process, will pave the way for novel and effective treatments for PD.