title: Antitumour and apoptotic effects of a novel Tris-peptide complex obtained after isolation of Raoultella ornithinolytica extracellular metabolites.
abstract: OBJECTIVE
  The characterization of the antitumour activity and chemical identification of the compounds obtained after the isolation of extracellular metabolites of bacteria Raoultella ornithinolytica.
  
  
  RESULTS
  The fraction with anticancer activity against the HeLa cell line, T47D and TOV-112D was obtained from the supernatants of R. ornithinolytica culture using ion-exchange chromatography, and separated by Sephadex G-50 medium gel filtration into two subfractions. The obtained compounds were analysed using Fourier Transform-Infrared Spectroscopy, Raman spectroscopy and matrix-assisted laser desorption/ionization MS/MS spectrometry. The antitumour activity of the two subfractions was analysed using 5-bromo-2-deoxy-uridine kit. The subfraction with the highest activity against HeLa cells was identified as Tris-peptide complex. The amino acid sequence of the peptide from the complex was found to be TDAPSFSDIPN and molecular weight was estimated at 1430·6576 Da. Cytotoxic, cytopathic and apoptotic effects in HeLa cells treated with the active complex were observed; however, the cytotoxic effect against normal human skin fibroblasts was minimal.
  
  
  CONCLUSIONS
  The Tris-peptide complex from R. ornithinolytica showed selective antitumour activity against the HeLa cell line.
  
  
  CONCLUSIONS
  The Tris-peptide complex due to the high selectivity can be used in biomedicine, and its derivatives may contribute to the development of new anticancer compounds.
authors: Department of Immunobiology, Institute of Biology and Biochemistry, Maria Curie-Skłodowska University, Lublin, Poland.
authors: M J
authors: MJ
authors: Fiołka
authors: Department of Biochemistry, Institute of Biology and Biochemistry, Maria Curie-Skłodowska University, Lublin, Poland.
authors: K
authors: K
authors: Grzywnowicz
authors: Department of Biology and Genetics, Medical University of Lublin, Poland.
authors: J
authors: J
authors: Rzymowska
authors: Department of Plant Anatomy and Cytology, Institute of Biology and Biochemistry, Maria Curie-Skłodowska University, Lublin, Poland.
authors: K
authors: K
authors: Lewtak
authors: Department of Biotechnology and Industrial Microbiology, Institute of Microbiology, Biotechnology and Immunology, University of Łódź, Poland.
authors: R
authors: R
authors: Szewczyk
authors: Analytical Laboratory, Faculty of Chemistry, Maria Curie-Skłodowska University, Lublin, Poland.
authors: E
authors: E
authors: Mendyk
authors: Analytical Laboratory, Faculty of Chemistry, Maria Curie-Skłodowska University, Lublin, Poland.
authors: R
authors: R
authors: Keller
mesh_terms: D000595:Amino Acid Sequence; D000970:Antineoplastic Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D017209:Apoptosis / Q000187:drug effects*; D045744:Cell Line, Tumor; D002850:Chromatography, Gel; D004755:Enterobacteriaceae / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D005347:Fibroblasts / Q000166:cytology / Q000187:drug effects; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D017550:Spectroscopy, Fourier Transform Infrared; D053719:Tandem Mass Spectrometry
chemical_list: D000970:Antineoplastic Agents; D010455:Peptides
keywords: anticancer; bioproduct; casein-derived peptide; earthworm; gut bacterium