Organic Letters
Organic Letters
5 years ago

Bulky Dehydroamino Acids Enhance Proteolytic Stability and Folding in β-Hairpin Peptides

Bulky Dehydroamino Acids Enhance Proteolytic Stability and Folding in β-Hairpin Peptides
Kei G. I. Webber, David W. Kastner, Ankur Jalan, Joshua L. Price, Steven L. Castle, Mason S. Smith
The bulky dehydroamino acids dehydrovaline (ΔVal) and dehydroethylnorvaline (ΔEnv) can be inserted into the turn regions of β-hairpin peptides without altering their secondary structures. These residues increase proteolytic stability, with ΔVal at the (i + 1) position having the most substantial impact. Additionally, a bulky dehydroamino acid can be paired with a d-amino acid (i.e., d-Pro) to synergistically enhance resistance to proteolysis. A link between proteolytic stability and peptide structure is established by the finding that a stabilized ΔVal-containing β-hairpin is more highly folded than its Asn-containing congener.

Publisher URL: http://dx.doi.org/10.1021/acs.orglett.7b02455

DOI: 10.1021/acs.orglett.7b02455

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