Foldamers are unnatural oligomers with a propensity to adopt well-defined conformations. These molecules have seen success in the mimicry of canonical peptide secondary structures such as -helices and -sheets. Current efforts in the field involve the application of foldamer design strategies to mimic higher-order protein structures and novel peptide architectures. Disulfide-rich peptides are notable candidates for foldamer research due to their intricate folding patterns and potent bioactivities. I am interested in establishing foldamer design principles for the synthesis of disulfide-rich peptide analogs with heterogeneous backbone modifications that manifest specific conformations, desired functionality and improved pharmacological properties.
B.S. in Microbiology, University of Hawaii at Manoa, 2008
M.S. in Molecular Biosciences and Bioengineering, University of Hawaii at Manoa, 2014
PhD Advisor: Dr. Seth Horne
Department of Chemistry
Chevron Science Center 1406
219 Parkman Avenue
- Werner HM, Cabalteja CC, Horne WS. (2015) Peptide Backbone Composition and Protease Susceptibility: Impact of Modification Type, Position, and Tandem Substitution. Chembiochem 2016, 17(8):712-8.
Cabalteja, C. C.; Mihalko, D. S.; Horne, W. S., Heterogeneous-Backbone Foldamer Mimics of a Computationally Designed, Disulfide-Rich Miniprotein. ChemBioChem 2019, 20 (1), 103-110.