| Literature DB >> 25262575 |
Yuliya Vasilyevna Danilova1, Elena Ilyasovna Shagimardanova1, Anna Borisovna Margulis1, Anna Aleksandrovna Toymentseva1, Nelly Pavlovna Balaban1, Nataliya Leonidovna Rudakova1, Albert Anatolyevich Rizvanov1, Margarita Rashidovna Sharipova2, András Palotás3.
Abstract
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.Entities:
Keywords: Aggregation; Alzheimer's disease; Bacillus pumilus; Bacterium; Proteinase; β-Amyloid-peptide
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Year: 2014 PMID: 25262575 DOI: 10.1016/j.brainresbull.2014.08.009
Source DB: PubMed Journal: Brain Res Bull ISSN: 0361-9230 Impact factor: 4.077