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Design of peptide inhibitors for Influenza A Non-structural Protein 1

by
Patrick Leonard Nosker
MS, Rutgers University, 2014
BA, Rutgers University, 2011

Thesis advisor: Vikas Nanda, Ph.D. & Gaetano Montelione, Ph.D.

Graduate Program in Biochemistry

Tuesday, July 12, 2016
2:00 p.m.


Abstract

Influenza A is responsible for tens of thousands of annual fatalities in the United States. The conventional medical strategy relies on prevention of infection using vaccines where are mildly effective at best and require yearly updates to reflect the expected prevalent strains, and anti-viral drugs for which there is significant clinical resistance. With this in mind, the non-structural protein 1 of influenza A (NS1A) is an appropriate target with high conservation and a multitude of anti-immune effects. It features an array of high surface area interactions which may be targetable using peptides.
We are developing molecular design tools to reliably create short (<20 amino acid) molecules with half-life and stability sufficient for drug-like function. In this thesis, I will explore D-amino acid motifs for increasing stability of peptides in the ideal Trp-cage peptide system and implement designed motifs in peptides designed to target the NS1A protein. Finally, we will demonstrate inhibition of the NS1A protein using our designed peptides.


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