Kazan (Volga region) Federal University, KFU
KAZAN
FEDERAL UNIVERSITY
 
BACTERIAL ENZYMES EFFECTIVELY DIGEST ALZHEIMER'S β-AMYLOID PEPTIDE
Form of presentationArticles in international journals and collections
Year of publication2014
  • Balaban Nelli Pavlovna, author
  • Danilova Yuliya Vasilevna, author
  • Margulis Anna Borisovna, author
  • Rudakova Natalya Leonidovna, author
  • Toymenceva Anna Aleksandrovna, author
  • Shagimardanova Elena Ilyasovna, author
  • Sharipova Margarita Rashidovna, author
  • Other authors Palotás A.
    Bibliographic description in the original language Danilova Y.V. Bacterial enzymes effectively digest Alzheimer's β-amyloid peptide / Y.V. Danilova, E.I. Shagimardanova, A.B. Margulis, A.A. Toymentseva, N.P. Balaban, N.L. Rudakova, A.A. Rizvanov, M.R. Sharipova, A. Palotás // Brain Res Bull. - 2014. V.108, No.1. - P.113-117.
    Annotation Aggregated β-amyloid peptides play key roles in the development of Alzheimer's disease, and recent evidence suggests that microbial particles, among others, can facilitate their polymerization. Bacterial enzymes, however, have been proved to be beneficial in degrading pathological fibrillar structures in clinical settings, such as strepto-kinases in resolving blood-clots. The purpose of this study was to investigate the ability of bacterial substances to effectively hydrolyze β-amyloid peptides. Degrading products of several proteinases from Bacillus pumilus were evaluated using MALDI-TOF mass-spectrometry, and their toxicity was assessed in vitro using cell-culture assays and morphological studies. These enzymes have proved to be non-toxic and were demonstrated to cleave through the functional domains of β-amyloid peptide. By yielding inactive fragments, proteinases of Bacillus pumilus may be used as candidate anti-amyloid agents.
    Keywords Bacillus pumilus, extracellular proteinases, Alzheimer's β-amyloid, MALDI-TOF mass-spectrometry
    The name of the journal BRAIN RES BULL
    Please use this ID to quote from or refer to the card https://repository.kpfu.ru/eng/?p_id=90036&p_lang=2

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