Form of presentation | Articles in international journals and collections |
Year of publication | 2014 |
Язык | русский |
|
Balaban Nelli Pavlovna, author
Margulis Anna Borisovna, author
Rudakova Natalya Leonidovna, author
Toymenceva Anna Aleksandrovna, author
Shagimardanova Elena Ilyasovna, author
Sharipova Margarita Rashidovna, author
|
Bibliographic description in the original language |
Danilova YV, Shagimardanova EI, Margulis AB, Toymentseva AA, Balaban NP, Rudakova NL, Rizvanov AA, Sharipova MR, Palotás A. Bacterial enzymes effectively digest Alzheimer's β-amyloid peptide.Brain Res Bull. 2014, 108, P.113-117. |
Annotation |
Aggregated
-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
-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
-
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=90034&p_lang=2 |
Full metadata record |
Field DC |
Value |
Language |
dc.contributor.author |
Balaban Nelli Pavlovna |
ru_RU |
dc.contributor.author |
Margulis Anna Borisovna |
ru_RU |
dc.contributor.author |
Rudakova Natalya Leonidovna |
ru_RU |
dc.contributor.author |
Toymenceva Anna Aleksandrovna |
ru_RU |
dc.contributor.author |
Shagimardanova Elena Ilyasovna |
ru_RU |
dc.contributor.author |
Sharipova Margarita Rashidovna |
ru_RU |
dc.date.accessioned |
2014-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2014-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2014 |
ru_RU |
dc.identifier.citation |
Danilova YV, Shagimardanova EI, Margulis AB, Toymentseva AA, Balaban NP, Rudakova NL, Rizvanov AA, Sharipova MR, Palotás A. Bacterial enzymes effectively digest Alzheimer's β-amyloid peptide.Brain Res Bull. 2014, 108, P.113-117. |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/eng/?p_id=90034&p_lang=2 |
ru_RU |
dc.description.abstract |
BRAIN RES BULL |
ru_RU |
dc.description.abstract |
Aggregated
-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
-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
-
amyloid peptide. By yielding inactive fragments, proteinases of Bacillus pumilus may be used as candidate
anti-amyloid agents. |
ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
Bacillus pumilus |
ru_RU |
dc.subject |
extracellular proteinases |
ru_RU |
dc.subject |
Alzheimer's β-amyloid |
ru_RU |
dc.subject |
MALDI-TOF mass-spectrometry |
ru_RU |
dc.title |
Bacterial enzymes effectively digest Alzheimer's β-amyloid peptide. |
ru_RU |
dc.type |
Articles in international journals and collections |
ru_RU |
|