Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis

The development of many severe human diseases is associated with the formation of amyloid fibrils. Most of the available information on the process of amyloid formation has been obtained from studies of small proteins and peptides, wherein the features of complex proteins’ aggregation remain insuffi...

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Autores principales:	Victor Marchenkov, Natalya Ryabova, Vitaly Balobanov, Anatoly Glukhov, Nelly Ilyina, Natalya Katina
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	amyloid carbonic anhydrase acid hydrolysis size-exclusion chromatography peptides Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/d49ca55a713547fdb77b66de98705753
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spelling	oai:doaj.org-article:d49ca55a713547fdb77b66de987057532021-11-25T16:52:45ZUnder Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis10.3390/biom111116082218-273Xhttps://doaj.org/article/d49ca55a713547fdb77b66de987057532021-10-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1608https://doaj.org/toc/2218-273XThe development of many severe human diseases is associated with the formation of amyloid fibrils. Most of the available information on the process of amyloid formation has been obtained from studies of small proteins and peptides, wherein the features of complex proteins’ aggregation remain insufficiently investigated. Our work aimed to research the amyloid aggregation of a large model protein, bovine carbonic anhydrase B (BCAB). It has previously been demonstrated that, when exposed to an acidic pH and elevated temperature, this protein forms amyloid fibrils. Here, we show that, under these conditions and before amyloid formation, BCAB undergoes fragmentation by acid hydrolysis to give free individual peptides and associated peptides. Fragments in associates contain a pronounced secondary structure and act as the main precursor of amyloid fibrils, wherein free peptides adopt mostly unstructured conformation and form predominantly irregular globular aggregates. Reduced acidity decreases the extent of acid hydrolysis, causing BCAB to form amorphous aggregates lacking the thioflavin T binding β-structure. The presented results provide new information on BCAB amyloid formation and show the importance of protein integrity control when working even in mildly acidic conditions.Victor MarchenkovNatalya RyabovaVitaly BalobanovAnatoly GlukhovNelly IlyinaNatalya KatinaMDPI AGarticleamyloidcarbonic anhydraseacid hydrolysissize-exclusion chromatographypeptidesMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1608, p 1608 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	amyloid carbonic anhydrase acid hydrolysis size-exclusion chromatography peptides Microbiology QR1-502
spellingShingle	amyloid carbonic anhydrase acid hydrolysis size-exclusion chromatography peptides Microbiology QR1-502 Victor Marchenkov Natalya Ryabova Vitaly Balobanov Anatoly Glukhov Nelly Ilyina Natalya Katina Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis
description	The development of many severe human diseases is associated with the formation of amyloid fibrils. Most of the available information on the process of amyloid formation has been obtained from studies of small proteins and peptides, wherein the features of complex proteins’ aggregation remain insufficiently investigated. Our work aimed to research the amyloid aggregation of a large model protein, bovine carbonic anhydrase B (BCAB). It has previously been demonstrated that, when exposed to an acidic pH and elevated temperature, this protein forms amyloid fibrils. Here, we show that, under these conditions and before amyloid formation, BCAB undergoes fragmentation by acid hydrolysis to give free individual peptides and associated peptides. Fragments in associates contain a pronounced secondary structure and act as the main precursor of amyloid fibrils, wherein free peptides adopt mostly unstructured conformation and form predominantly irregular globular aggregates. Reduced acidity decreases the extent of acid hydrolysis, causing BCAB to form amorphous aggregates lacking the thioflavin T binding β-structure. The presented results provide new information on BCAB amyloid formation and show the importance of protein integrity control when working even in mildly acidic conditions.
format	article
author	Victor Marchenkov Natalya Ryabova Vitaly Balobanov Anatoly Glukhov Nelly Ilyina Natalya Katina
author_facet	Victor Marchenkov Natalya Ryabova Vitaly Balobanov Anatoly Glukhov Nelly Ilyina Natalya Katina
author_sort	Victor Marchenkov
title	Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis
title_short	Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis
title_full	Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis
title_fullStr	Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis
title_full_unstemmed	Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis
title_sort	under conditions of amyloid formation bovine carbonic anhydrase b undergoes fragmentation by acid hydrolysis
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/d49ca55a713547fdb77b66de98705753
work_keys_str_mv	AT victormarchenkov underconditionsofamyloidformationbovinecarbonicanhydrasebundergoesfragmentationbyacidhydrolysis AT natalyaryabova underconditionsofamyloidformationbovinecarbonicanhydrasebundergoesfragmentationbyacidhydrolysis AT vitalybalobanov underconditionsofamyloidformationbovinecarbonicanhydrasebundergoesfragmentationbyacidhydrolysis AT anatolyglukhov underconditionsofamyloidformationbovinecarbonicanhydrasebundergoesfragmentationbyacidhydrolysis AT nellyilyina underconditionsofamyloidformationbovinecarbonicanhydrasebundergoesfragmentationbyacidhydrolysis AT natalyakatina underconditionsofamyloidformationbovinecarbonicanhydrasebundergoesfragmentationbyacidhydrolysis
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Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis

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