Antimicrobial Peptide Mastoparan-AF Kills Multi-Antibiotic Resistant Escherichia coli O157:H7 via Multiple Membrane Disruption Patterns and Likely by Adopting 3–11 Amphipathic Helices to Favor Membrane Interaction

• Published in: Membranes (Basel) Vol. 13; no. 2; p. 251
• Main Authors: Lin, Chun-Hsien, Shyu, Ching-Lin, Wu, Zong-Yen, Wang, Chao-Min, Chiou, Shiow-Her, Chen, Jiann-Yeu, Tseng, Shu-Ying, Lin, Ting-Er, Yuan, Yi-Po, Ho, Shu-Peng, Tung, Kwong-Chung, Mao, Frank Chiahung, Lee, Han-Jung, Tu, Wu-Chun
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 20.02.2023; MDPI
• Subjects: 5' Untranslated regions; Amino acids; Antibiotic resistance; Antibiotics; Anticoagulants; Antiinfectives and antibacterials; Antimicrobial activity; Antimicrobial agents; antimicrobial peptide; Antimicrobial peptides; Bacteria; Blood; Clinical isolates; Cloning; Disruption; Drug resistance; E coli; Escherichia coli; Escherichia coli O157:H7; Helices; Hydrophobicity; Lipids; Mastoparan; mastoparan-AF; membrane disruption pattern; membrane permeabilization; Membranes; Microscopy; Pathogens; Physicochemical properties; Polypeptides; Sodium; Tubes; Zoonoses; United States > US; Taiwan; Vespa affinis; antibiotic resistance; mastoparan-AF; membrane disruption pattern; membrane permeabilization; antimicrobial peptide; Escherichia coli O157:H7

We investigated the antimicrobial activity and membrane disruption modes of the antimicrobial peptide mastoparan-AF against hemolytic Escherichia coli O157:H7. Based on the physicochemical properties, mastoparan-AF may potentially adopt a 3–11 amphipathic helix-type structure, with five to seven non...