University of Hertfordshire

  • Hermine Mkrtchyan
  • Simon Gibbons
  • Sibylle Heidelberger
  • Mire Zloh
  • Hamidreza Khalatbari Limaki
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Original languageEnglish
Pages (from-to)255-60
Number of pages6
JournalInternational Journal of Antimicrobial Agents
Publication statusPublished - 2010


In the last two decades, antimicrobial peptides (AMPs) have been gaining attention as antimicrobial alternatives to chemical food preservatives and commonly used antibiotics. Lactobacillus acidophilus n.v. Er 317/402 strain Narine produces a small AMP with a molecular weight of 1.1kDa, designated acidocin LCHV. In this study, the AMP was extremely heat stable (90min at 130 degrees C), was active over a wide pH range and was found to be sensitive to proteolytic enzymes (trypsin, pepsin and proteinase K). Acidocin LCHV has a broad spectrum of activity both against Gram-positive and Gram-negative pathogens, including several that are classified as Especially Dangerous Infections by the World Health Organization as well as meticillin-resistant Staphylococcus aureus (MRSA) and Clostridium difficile. Matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOF/MS) was used to determine the molecular mass and sequence of the purified peptide. Complete killing with immediate impact on cells was observed within a very short period of time (10min).


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