Chemoenzymatic Platforms for the Discovery of New Peptide Therapeutics

Albert Bowers

Professor, University of North Carolina at Chapel Hill

ABSTRACT

RiPPs are a rapidly growing class of peptide derived natural products. RiPP enzymes carry out remarkable chemistry en route to transforming short peptides into bioactive molecules. We have recently developed new technology for generating large and diverse libraries of RiPP natural products based on the promiscuity of key biosynthetic enzymes from RiPP pathways. Two examples will be presented. First, by employing members of the new pyridine synthase family of macrocyclases, discovered in our lab, we create non-natural analogues of the potent anti-MRSA antibiotics known as thiopeptides to explore their structure activity relationships. Second, we exploit the sactionine synthase AlbA from Bacillus subtilis to design stapled alpha-helical mimics for the inhibition of key therapeutic targets.

BIO

Born and raised in New Jersey, Dr. Bowers obtained his BA from the University of Chicago and went on to complete his Ph.D. in organic chemistry in 2007, at the University of Illinois at Chicago, under the guidance of Prof. David Crich. He was an NIH postdoctoral fellow in the labs of Professor Robert M. Williams at Colorado State University and Professor Christopher T. Walsh at Harvard Medical School. Aer spending a year as Assistant Professor at Purdue University, he joined the faculty of Chemical Biology and Medicinal Chemistry at the University of North Carolina at Chapel Hill in 2012. His lab engineers biosynthetic pathways and develops chemoenzymatic strategies to generate next-generation therapeutics.