Sequence determinants of protein aggregation: tools to increase protein solubility

Abstract Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein productio...
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Autor*in:	Ventura, Salvador [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2005

Schlagwörter:	Protein Aggregation Amyloid Fibril Native Conformation Recombinant Protein Expression Folding Intermediate

Anmerkung:	© Ventura; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (

Übergeordnetes Werk:	Enthalten in: Microbial cell factories - London : Biomed Central, 2002, 4(2005), 1 vom: 22. Apr.
Übergeordnetes Werk:	volume:4 ; year:2005 ; number:1 ; day:22 ; month:04

Links:	Volltext

DOI / URN:	10.1186/1475-2859-4-11

Katalog-ID:	SPR028553640

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allfields	10.1186/1475-2859-4-11 doi (DE-627)SPR028553640 (SPR)1475-2859-4-11-e DE-627 ger DE-627 rakwb eng Ventura, Salvador verfasserin aut Sequence determinants of protein aggregation: tools to increase protein solubility 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Ventura; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Abstract Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein production and are hampering the development of top priority research areas such structural genomics. Inclusion body formation was formerly considered to occur via non-specific association of hydrophobic surfaces in folding intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria resembles to the well-studied process of amyloid fibril formation. Both processes appear to rely on the formation of specific, sequence-dependent, intermolecular interactions driving the formation of structured protein aggregates. This similarity in the mechanisms of aggregation will probably allow applying anti-aggregational strategies already tested in the amyloid context to the less explored area of protein aggregation inside bacteria. Specifically, new sequence-based approaches appear as promising tools to tune protein aggregation in biotechnological processes. Protein Aggregation (dpeaa)DE-He213 Amyloid Fibril (dpeaa)DE-He213 Native Conformation (dpeaa)DE-He213 Recombinant Protein Expression (dpeaa)DE-He213 Folding Intermediate (dpeaa)DE-He213 Enthalten in Microbial cell factories London : Biomed Central, 2002 4(2005), 1 vom: 22. Apr. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:4 year:2005 number:1 day:22 month:04 https://dx.doi.org/10.1186/1475-2859-4-11 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1 22 04
spelling	10.1186/1475-2859-4-11 doi (DE-627)SPR028553640 (SPR)1475-2859-4-11-e DE-627 ger DE-627 rakwb eng Ventura, Salvador verfasserin aut Sequence determinants of protein aggregation: tools to increase protein solubility 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Ventura; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Abstract Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein production and are hampering the development of top priority research areas such structural genomics. Inclusion body formation was formerly considered to occur via non-specific association of hydrophobic surfaces in folding intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria resembles to the well-studied process of amyloid fibril formation. Both processes appear to rely on the formation of specific, sequence-dependent, intermolecular interactions driving the formation of structured protein aggregates. This similarity in the mechanisms of aggregation will probably allow applying anti-aggregational strategies already tested in the amyloid context to the less explored area of protein aggregation inside bacteria. Specifically, new sequence-based approaches appear as promising tools to tune protein aggregation in biotechnological processes. Protein Aggregation (dpeaa)DE-He213 Amyloid Fibril (dpeaa)DE-He213 Native Conformation (dpeaa)DE-He213 Recombinant Protein Expression (dpeaa)DE-He213 Folding Intermediate (dpeaa)DE-He213 Enthalten in Microbial cell factories London : Biomed Central, 2002 4(2005), 1 vom: 22. Apr. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:4 year:2005 number:1 day:22 month:04 https://dx.doi.org/10.1186/1475-2859-4-11 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1 22 04
allfields_unstemmed	10.1186/1475-2859-4-11 doi (DE-627)SPR028553640 (SPR)1475-2859-4-11-e DE-627 ger DE-627 rakwb eng Ventura, Salvador verfasserin aut Sequence determinants of protein aggregation: tools to increase protein solubility 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Ventura; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Abstract Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein production and are hampering the development of top priority research areas such structural genomics. Inclusion body formation was formerly considered to occur via non-specific association of hydrophobic surfaces in folding intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria resembles to the well-studied process of amyloid fibril formation. Both processes appear to rely on the formation of specific, sequence-dependent, intermolecular interactions driving the formation of structured protein aggregates. This similarity in the mechanisms of aggregation will probably allow applying anti-aggregational strategies already tested in the amyloid context to the less explored area of protein aggregation inside bacteria. Specifically, new sequence-based approaches appear as promising tools to tune protein aggregation in biotechnological processes. Protein Aggregation (dpeaa)DE-He213 Amyloid Fibril (dpeaa)DE-He213 Native Conformation (dpeaa)DE-He213 Recombinant Protein Expression (dpeaa)DE-He213 Folding Intermediate (dpeaa)DE-He213 Enthalten in Microbial cell factories London : Biomed Central, 2002 4(2005), 1 vom: 22. Apr. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:4 year:2005 number:1 day:22 month:04 https://dx.doi.org/10.1186/1475-2859-4-11 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1 22 04
allfieldsGer	10.1186/1475-2859-4-11 doi (DE-627)SPR028553640 (SPR)1475-2859-4-11-e DE-627 ger DE-627 rakwb eng Ventura, Salvador verfasserin aut Sequence determinants of protein aggregation: tools to increase protein solubility 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Ventura; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Abstract Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein production and are hampering the development of top priority research areas such structural genomics. Inclusion body formation was formerly considered to occur via non-specific association of hydrophobic surfaces in folding intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria resembles to the well-studied process of amyloid fibril formation. Both processes appear to rely on the formation of specific, sequence-dependent, intermolecular interactions driving the formation of structured protein aggregates. This similarity in the mechanisms of aggregation will probably allow applying anti-aggregational strategies already tested in the amyloid context to the less explored area of protein aggregation inside bacteria. Specifically, new sequence-based approaches appear as promising tools to tune protein aggregation in biotechnological processes. Protein Aggregation (dpeaa)DE-He213 Amyloid Fibril (dpeaa)DE-He213 Native Conformation (dpeaa)DE-He213 Recombinant Protein Expression (dpeaa)DE-He213 Folding Intermediate (dpeaa)DE-He213 Enthalten in Microbial cell factories London : Biomed Central, 2002 4(2005), 1 vom: 22. Apr. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:4 year:2005 number:1 day:22 month:04 https://dx.doi.org/10.1186/1475-2859-4-11 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1 22 04
allfieldsSound	10.1186/1475-2859-4-11 doi (DE-627)SPR028553640 (SPR)1475-2859-4-11-e DE-627 ger DE-627 rakwb eng Ventura, Salvador verfasserin aut Sequence determinants of protein aggregation: tools to increase protein solubility 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Ventura; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Abstract Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein production and are hampering the development of top priority research areas such structural genomics. Inclusion body formation was formerly considered to occur via non-specific association of hydrophobic surfaces in folding intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria resembles to the well-studied process of amyloid fibril formation. Both processes appear to rely on the formation of specific, sequence-dependent, intermolecular interactions driving the formation of structured protein aggregates. This similarity in the mechanisms of aggregation will probably allow applying anti-aggregational strategies already tested in the amyloid context to the less explored area of protein aggregation inside bacteria. Specifically, new sequence-based approaches appear as promising tools to tune protein aggregation in biotechnological processes. Protein Aggregation (dpeaa)DE-He213 Amyloid Fibril (dpeaa)DE-He213 Native Conformation (dpeaa)DE-He213 Recombinant Protein Expression (dpeaa)DE-He213 Folding Intermediate (dpeaa)DE-He213 Enthalten in Microbial cell factories London : Biomed Central, 2002 4(2005), 1 vom: 22. Apr. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:4 year:2005 number:1 day:22 month:04 https://dx.doi.org/10.1186/1475-2859-4-11 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1 22 04
language	English
source	Enthalten in Microbial cell factories 4(2005), 1 vom: 22. Apr. volume:4 year:2005 number:1 day:22 month:04
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topic_facet	Protein Aggregation Amyloid Fibril Native Conformation Recombinant Protein Expression Folding Intermediate
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container_title	Microbial cell factories
authorswithroles_txt_mv	Ventura, Salvador @@aut@@
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spellingShingle	Ventura, Salvador misc Protein Aggregation misc Amyloid Fibril misc Native Conformation misc Recombinant Protein Expression misc Folding Intermediate Sequence determinants of protein aggregation: tools to increase protein solubility
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topic_title	Sequence determinants of protein aggregation: tools to increase protein solubility Protein Aggregation (dpeaa)DE-He213 Amyloid Fibril (dpeaa)DE-He213 Native Conformation (dpeaa)DE-He213 Recombinant Protein Expression (dpeaa)DE-He213 Folding Intermediate (dpeaa)DE-He213
topic	misc Protein Aggregation misc Amyloid Fibril misc Native Conformation misc Recombinant Protein Expression misc Folding Intermediate
topic_unstemmed	misc Protein Aggregation misc Amyloid Fibril misc Native Conformation misc Recombinant Protein Expression misc Folding Intermediate
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title_sort	sequence determinants of protein aggregation: tools to increase protein solubility
title_auth	Sequence determinants of protein aggregation: tools to increase protein solubility
abstract	Abstract Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein production and are hampering the development of top priority research areas such structural genomics. Inclusion body formation was formerly considered to occur via non-specific association of hydrophobic surfaces in folding intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria resembles to the well-studied process of amyloid fibril formation. Both processes appear to rely on the formation of specific, sequence-dependent, intermolecular interactions driving the formation of structured protein aggregates. This similarity in the mechanisms of aggregation will probably allow applying anti-aggregational strategies already tested in the amyloid context to the less explored area of protein aggregation inside bacteria. Specifically, new sequence-based approaches appear as promising tools to tune protein aggregation in biotechnological processes. © Ventura; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstractGer	Abstract Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein production and are hampering the development of top priority research areas such structural genomics. Inclusion body formation was formerly considered to occur via non-specific association of hydrophobic surfaces in folding intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria resembles to the well-studied process of amyloid fibril formation. Both processes appear to rely on the formation of specific, sequence-dependent, intermolecular interactions driving the formation of structured protein aggregates. This similarity in the mechanisms of aggregation will probably allow applying anti-aggregational strategies already tested in the amyloid context to the less explored area of protein aggregation inside bacteria. Specifically, new sequence-based approaches appear as promising tools to tune protein aggregation in biotechnological processes. © Ventura; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstract_unstemmed	Abstract Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein production and are hampering the development of top priority research areas such structural genomics. Inclusion body formation was formerly considered to occur via non-specific association of hydrophobic surfaces in folding intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria resembles to the well-studied process of amyloid fibril formation. Both processes appear to rely on the formation of specific, sequence-dependent, intermolecular interactions driving the formation of structured protein aggregates. This similarity in the mechanisms of aggregation will probably allow applying anti-aggregational strategies already tested in the amyloid context to the less explored area of protein aggregation inside bacteria. Specifically, new sequence-based approaches appear as promising tools to tune protein aggregation in biotechnological processes. © Ventura; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
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title_short	Sequence determinants of protein aggregation: tools to increase protein solubility
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Sequence determinants of protein aggregation: tools to increase protein solubility

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