The solution NMR structure of cis-dicarba-brevinin-1BYa in 33% trifluoroethanol
Insights into conformation and membrane interactions of the acyclic and dicarba-bridged brevinin-1BYa antimicrobial peptides.
Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii.
Synthesis, conformational analysis and biological properties of a dicarba derivative of the antimicrobial peptide, brevinin-1BYa.
AGL = allylglycine An intramolecular vinylic bond exists between the residues AGL-18 and AGL-24.
The solution NMR structure of dicarba-brevinin-1BYa in 33% trifluoroethanol
1.35 mM NA- dicarba-brevinin-1BYa, trifluoroethanol/water
cationic, rana-box, antimicrobial peptide, ANTIMICROBIAL PROTEIN