Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa

Anticancer mechanisms of action of two small amphipathic β2,2-amino acid derivatives derived from antimicrobial peptides

(2012) Dominik Ausbacher et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Characterization of dual effects induced by antimicrobial peptides: Regulated cell death or membrane disruption

(2012) Edgar J. Paredes-Gamero et al.   BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS

Antitumor effects and cell selectivity of temporin-1CEa, an antimicrobial peptide from the skin secretions of the Chinese brown frog (Rana chensinensis)

(2011) Che Wang et al.   BIOCHIMIE

Rational Design of α-Helical Antimicrobial Peptides to Target Gram-negative Pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: Utilization of Charge, ‘Specificity Determinants,’ Total Hydrophobicity, Hydrophobe Type and Location as Design Para

(2011) Ziqing Jiang et al.   Chemical Biology & Drug Design

Studies on Mechanism of Action of Anticancer Peptides by Modulation of Hydrophobicity Within a Defined Structural Framework

(2011) Y.-b. Huang et al.   MOLECULAR CANCER THERAPEUTICS

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

Studies on anticancer activities of antimicrobial peptides

(2007) David W. Hoskin et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES