β-Strand Mimics based on Tetrahydropyridazinedione (tpd) Peptide Stitching

Authors

Chang Won Kang, University of South Florida
Matthew P. Sarnowski, University of South Florida
Sujeewa Ranatunga, University of South Florida
Lukasz Wojtas, University of South FloridaFollow
Rainer S. Metcalf, University of South Florida
Wayne C. Guida, University of South FloridaFollow
Juan R. Del Valle, University of South Florida

Document Type

Article

Publication Date

2015

Digital Object Identifier (DOI)

https://doi.org/10.1039/C5CC07189E

Abstract

Short peptides featuring a tetrahydropyridazinedione (tpd) backbone tether exhibit reduced conformational flexibility external to the heterocyclic constraint. Analysis by NMR, molecular modeling and X-ray crystallography suggests both covalent and non-covalent stabilization of extended peptide conformations. An efficient solid-phase protocol was developed for the synthesis of a new class of β-strand mimics based on oligomeric tpd subunits.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Chemical Communication, v. 51, p. 16259-16262

Scholar Commons Citation

Kang, Chang Won; Sarnowski, Matthew P.; Ranatunga, Sujeewa; Wojtas, Lukasz; Metcalf, Rainer S.; Guida, Wayne C.; and Del Valle, Juan R., "β-Strand Mimics based on Tetrahydropyridazinedione (tpd) Peptide Stitching" (2015). Chemistry Faculty Publications. 154.
https://digitalcommons.usf.edu/chm_facpub/154