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

ABSTRACT: The bulky dehydroamino acids dehydrovaline (?Val) and dehydroethylnorvaline (?Env) can be inserted into the turn regions of ?-hairpin peptides without altering their secondary structures. These residues increase proteolytic stability, with ?Val 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 ?Val-containing ?-hairpin is more highly folded than its Asn-containing congener.

SUBMITTER: Jalan A 

PROVIDER: S-EPMC6085080 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature