Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence

• Published in: Molecules (Basel, Switzerland) Vol. 26; no. 2; p. 444
• Main Authors: Hirano, Motoharu, Saito, Chihiro, Yokoo, Hidetomo, Goto, Chihiro, Kawano, Ryuji, Misawa, Takashi, Demizu, Yosuke
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 16.01.2021; MDPI
• Subjects: Amino Acid Sequence; Amino acids; amphipathicity; Animals; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - pharmacology; Antimicrobial agents; antimicrobial peptides; Aqueous solutions; Bacteria; Chromatography; Cytotoxicity; Drug resistance; Enzymes; Gram-negative bacteria; Gram-Negative Bacteria - growth & development; Gram-Positive Bacteria - growth & development; helical structure; Hydrocarbons; magainin 2; Magainins - chemistry; Magainins - pharmacology; Membranes; Peptides; stapled peptide; Xenopus laevis; Xenopus Proteins - chemistry; Xenopus Proteins - pharmacology; stapled peptide; amphipathicity; antimicrobial peptides; helical structure; magainin 2

Magainin 2 (Mag2), which was isolated from the skin of the African clawed frog, is a representative antimicrobial peptide (AMP) that exerts antimicrobial activity via microbial membrane disruption. It has been reported that the helicity and amphipathicity of Mag2 play important roles in its antimicr...