Investigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action

Design of Potent, Non-Toxic Antimicrobial Agents Based upon the Structure of the Frog Skin Peptide, Temporin-1CEb from Chinese Brown Frog, Rana chensinensis

(2012) Dejing Shang et al.   Chemical Biology & Drug Design

Structure−Activity Relationships of Piscidin 4, a Piscine Antimicrobial Peptide

(2011) N. G. Park et al.   BIOCHEMISTRY

Membrane interaction and antibacterial properties of two mildly cationic peptide diastereomers, bombinins H2 and H4, isolated from Bombina skin

(2011) Cristina Coccia et al.   EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS

Structural flexibility and the positive charges are the key factors in bacterial cell selectivity and membrane penetration of peptoid-substituted analog of Piscidin 1

(2010) Jin-Kyoung Kim et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: Comparison with other hydrophilicity/hydrophobicity scales

(2009) Colin T. Mant et al.   BIOPOLYMERS

Molecular Cloning of cDNAs Encoding Antimicrobial Peptide Precursors from the Skin of the Chinese Brown Frog,Rana chensinensis

(2009) Dejing Shang et al.   ZOOLOGICAL SCIENCE