Bulky Dehydroamino Acids Enhance Proteolytic Stability and Folding in β‑Hairpin Peptides
Published on 2017-09-14T15:04:08Z (GMT) by
The bulky dehydroamino acids dehydrovaline (ΔVal) and dehydroethylnorvaline (Δ<i>E</i>nv) 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>i</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.
Cite this collection
Jalan, Ankur; Kastner, David W.; Webber, Kei G. I.; Smith, Mason S.; Price, Joshua L.; Castle, Steven L. (2017): Bulky Dehydroamino Acids Enhance Proteolytic Stability
and Folding in β‑Hairpin Peptides. ACS Publications. Collection.