Soluble variants of human recombinant glutaminyl cyclase.
Recombinant human Glutaminyl Cyclase expressed in E. coli is produced as inclusion bodies. Lack of glycosylation is the main origin of its accumulation in insoluble aggregates. Mutation of single isolated hydrophobic amino acids into negative amino acids was not able to circumvent inclusion bodies f...
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2013
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oai:doaj.org-article:08b72f1f483a4db7a361c7e1338f8eac2021-11-18T08:59:25ZSoluble variants of human recombinant glutaminyl cyclase.1932-620310.1371/journal.pone.0071657https://doaj.org/article/08b72f1f483a4db7a361c7e1338f8eac2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23977104/?tool=EBIhttps://doaj.org/toc/1932-6203Recombinant human Glutaminyl Cyclase expressed in E. coli is produced as inclusion bodies. Lack of glycosylation is the main origin of its accumulation in insoluble aggregates. Mutation of single isolated hydrophobic amino acids into negative amino acids was not able to circumvent inclusion bodies formation. On the contrary, substitution with carboxyl-terminal residues of two or three aromatic residues belonging to extended hydrophobic patches on the protein surface provided soluble but still active forms of the protein. These mutants could be expressed in isotopically enriched forms for NMR studies and the maximal attainable concentration was sufficient for the acquisition of (1)H-(15)N HSQC spectra that represent the starting point for future drug development projects targeting Alzheimer's disease.Cristiana CastaldoSilvia CiambellottiRaquel de Pablo-LatorreDaniela LalliValentina PorcariPaola TuranoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 8, p e71657 (2013) |
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Medicine R Science Q Cristiana Castaldo Silvia Ciambellotti Raquel de Pablo-Latorre Daniela Lalli Valentina Porcari Paola Turano Soluble variants of human recombinant glutaminyl cyclase. |
description |
Recombinant human Glutaminyl Cyclase expressed in E. coli is produced as inclusion bodies. Lack of glycosylation is the main origin of its accumulation in insoluble aggregates. Mutation of single isolated hydrophobic amino acids into negative amino acids was not able to circumvent inclusion bodies formation. On the contrary, substitution with carboxyl-terminal residues of two or three aromatic residues belonging to extended hydrophobic patches on the protein surface provided soluble but still active forms of the protein. These mutants could be expressed in isotopically enriched forms for NMR studies and the maximal attainable concentration was sufficient for the acquisition of (1)H-(15)N HSQC spectra that represent the starting point for future drug development projects targeting Alzheimer's disease. |
format |
article |
author |
Cristiana Castaldo Silvia Ciambellotti Raquel de Pablo-Latorre Daniela Lalli Valentina Porcari Paola Turano |
author_facet |
Cristiana Castaldo Silvia Ciambellotti Raquel de Pablo-Latorre Daniela Lalli Valentina Porcari Paola Turano |
author_sort |
Cristiana Castaldo |
title |
Soluble variants of human recombinant glutaminyl cyclase. |
title_short |
Soluble variants of human recombinant glutaminyl cyclase. |
title_full |
Soluble variants of human recombinant glutaminyl cyclase. |
title_fullStr |
Soluble variants of human recombinant glutaminyl cyclase. |
title_full_unstemmed |
Soluble variants of human recombinant glutaminyl cyclase. |
title_sort |
soluble variants of human recombinant glutaminyl cyclase. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2013 |
url |
https://doaj.org/article/08b72f1f483a4db7a361c7e1338f8eac |
work_keys_str_mv |
AT cristianacastaldo solublevariantsofhumanrecombinantglutaminylcyclase AT silviaciambellotti solublevariantsofhumanrecombinantglutaminylcyclase AT raqueldepablolatorre solublevariantsofhumanrecombinantglutaminylcyclase AT danielalalli solublevariantsofhumanrecombinantglutaminylcyclase AT valentinaporcari solublevariantsofhumanrecombinantglutaminylcyclase AT paolaturano solublevariantsofhumanrecombinantglutaminylcyclase |
_version_ |
1718421063986053120 |