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Ramaiah Muthyala

Portrait - Dwight Anderson, PhD

Research Associate Professor

Medicinal Chemistry, Pharmacy
Member, Center for Drug Design

Email: muthy003@umn.edu
Phone: (612) 624-7120

Education

Ph.D., University of Sagar, India, 1968
Ph.D., University of East Anglia, England, 1975

Research Interests

The direction of Dr. Muthyala's research program is to focus on biological and chemical information to transform biologically active molecules into useful drugs. The drug design process will combine:

  • Structural information from proteins
  • Enzyme studies using computer modeling
  • Synthetic methods to build molecules

Antibacterials

Over the last two decades, drug resistant strains of bacteria have increased, while the discovery and design of new and effective antibacterial agents by the drug industry have not kept up pace. Our focus is to identify novel chemotherapeutic agents based on well-recognized cell wall biosynthetic processes of the bacterial life cycle. Of great concern is the emergence of resistant bacterial strains to vancomycin, the last line of defense against severe infection, especially when all else fails. Our strategy is to design an antibiotic that will overcome this resistance and become a replacement for this drug.

Neurological Disorders

The cholinergic hypothesis states that Alzheimer's Disease is caused by the poor functioning of acetylcholine, a brain chemical important for learning and memory. This hypothesis has led to perhaps the only successful drug treatment for Alzheimer's Disease, using molecules which block acetylcholinesterase, a protein which processes acetylcholine. We are therefore searching for novel, potent, and selective inhibitors that target acetylcholinesterase.

Neuro-degeneration in Alzheimer's may be caused by the deposition of amyloid protein in brain tissue. The amyloid precursor protein is converted to amyloid protein by a-, b-, and g- secretases. Recent advances in the study of secretases have allowed us to propose selective inhibitors that might block formation of the amyloid protein.


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