Influence of adding terminal tags on the structural and antimicrobial properties of the peptide caerin 1.1

摘要: Abstract Aquaculture is threatened by severe bacterial and viral outbreaks which can cause massive mortality limit productivity. Antimicrobial peptides are a promising tool for the control of infectious diseases; however, their use in aquaculture sector has been poorly explored. Recombinant production an interesting alternative to chemical synthesis, still important challenges address. Although extra amino acid tags usually added ends recombinant proteins enhance stability facilitate purification or translational processing, effect these on function antimicrobial completely unknown. This particularly case short cationic peptide caerin, originally isolated from frog skin secretions, other bioactivity directly related with its ability adopt amphipathic alpha-helical structure upon interaction microbial membranes. Caerin demonstrated bactericidal activity against several human pathogens, however over usual pathogens remains practically unexplored. In present work, we have studied adding terminal tag polyhistidine (6xHis) 2A foot mouth disease virus (FMDV-2A) N- C- terminus caerin collection common species. addition, composed two tandem consecutive sequences investigated. We concluded that addition causes drastic reduction antiviral viruses depends target However, 6xHis extension at N maintains increases most fish pathogenic bacteria tested. According our data, there only moderate agreement between theoretical predictions obtained silico models experimental observations. information essential rational design strategies aim peptides, be used as anti-infective agents aquaculture.