The solution NMR structure of cis-dicarba-brevinin-1BYa in sodium dodecyl sulphate micelles
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 sodium dodecyl sulphate micelles
1.5 mM NA- dicarba-brevinin-1BYa, 230 mM sodium dodecyl sulfphate, 90% H2O/10% D2O
UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN
cationic, rana-box, antimicrobial peptide, ANTIMICROBIAL PROTEIN