Sunil Kumar, PhD

Sunil Kumar – Research Investigator

Investigator:

Sunil Kumar, PhD

Name of Institution:

University of Denver, Denver, CO

Project Title:

Identification of novel targets associated with α-synuclein aggregation


Investigator Bio:

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, including synthetic, biophysical, and in vivo, to gain mechanistic and therapeutic insights into various amyloid disease, including Parkinson’s disease (PD) and cancer.

Objective:

To identify α-Synuclein (αS) sequence based novel targets that are essential for αS oligomerization and aggregation processes which are directly associated with PD.

Background:

PD is a progressive neurodegenerative disorder for which there is no successful prevention or intervention. The pathological hallmark for PD involves the aggregation of functional αS into non-functional amyloid structures. Therefore, modulation of αS aggregation is a promising therapeutic intervention for PD. One of the potential therapeutic interventions against PD is the effective inhibition of αS aggregation. However, the bottleneck towards achieving this goal is the identification of the αS sequences that are essential for oligomerization and aggregation.

Methods/Design:

We will use a biochemical approach in tandem with numerous in vitro and in vivo PD models to identify αS sequences and their structural features which mediate the formation of neurotoxic αS oligomers/fibers.

Relevance to Diagnosis/Treatment of Parkinson’s disease:

This proposed study aims to identify novel targets associated with the aggregation of αS, a process central to the onset of PD. We anticipate that the identification of these new targets will pave the way for novel and effective treatments for PD.