Computational study of elements of stability of a four-helix bundle protein biosurfactant
Biosurfactants are surface-active molecules produced principally by microorganisms. They are a sustainable alternative to chemically-synthesized surfactants, having the advantages of being non-toxic, highly functional, eco-friendly and biodegradable. However they are currently only used in a few ind...
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| creator | Schaller, Andrea Connors, Natalie K. Dwyer, Mirjana Dimitrijev Oelmeier, Stefan A. Hubbuch, Jürgen Middelberg, Anton P. J. |
| description | Biosurfactants are surface-active molecules produced principally by microorganisms. They are a sustainable alternative to chemically-synthesized surfactants, having the advantages of being non-toxic, highly functional, eco-friendly and biodegradable. However they are currently only used in a few industrial products due to costs associated with production and purification, which exceed those for commodity chemical surfactants. DAMP4, a member of a four-helix bundle biosurfactant protein family, can be produced in soluble form and at high yield in
Escherichia coli
, and can be recovered using a facile thermal phase-separation approach. As such, it encompasses an interesting synergy of biomolecular and chemical engineering with prospects for low-cost production even for industrial sectors. DAMP4 is highly functional, and due to its extraordinary thermal stability it can be purified in a simple two-step process, in which the combination of high temperature and salt leads to denaturation of all contaminants, whereas DAMP4 stays stable in solution and can be recovered by filtration. This study aimed to characterize and understand the fundamental drivers of DAMP4 stability to guide further process and surfactant design studies. The complementary use of experiments and molecular dynamics simulation revealed a broad pH and temperature tolerance for DAMP4, with a melting point of 122.4 °C, suggesting the hydrophobic core as the major contributor to thermal stability. Simulation of systematically created in silico variants of DAMP4 showed an influence of number and location of hydrophilic mutations in the hydrophobic core on stability, demonstrating a tolerance of up to three mutations before a strong loss in stability occurred. The results suggest a consideration of a balance of stability, functionality and kinetics for new designs according to their application, aiming for maximal functionality but at adequate stability to allow for cost-efficient production using thermal phase separation approaches. |
| doi_str_mv | 10.1007/s10822-014-9803-6 |
| format | Article |
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Escherichia coli
, and can be recovered using a facile thermal phase-separation approach. As such, it encompasses an interesting synergy of biomolecular and chemical engineering with prospects for low-cost production even for industrial sectors. DAMP4 is highly functional, and due to its extraordinary thermal stability it can be purified in a simple two-step process, in which the combination of high temperature and salt leads to denaturation of all contaminants, whereas DAMP4 stays stable in solution and can be recovered by filtration. This study aimed to characterize and understand the fundamental drivers of DAMP4 stability to guide further process and surfactant design studies. The complementary use of experiments and molecular dynamics simulation revealed a broad pH and temperature tolerance for DAMP4, with a melting point of 122.4 °C, suggesting the hydrophobic core as the major contributor to thermal stability. Simulation of systematically created in silico variants of DAMP4 showed an influence of number and location of hydrophilic mutations in the hydrophobic core on stability, demonstrating a tolerance of up to three mutations before a strong loss in stability occurred. The results suggest a consideration of a balance of stability, functionality and kinetics for new designs according to their application, aiming for maximal functionality but at adequate stability to allow for cost-efficient production using thermal phase separation approaches.</description><identifier>ISSN: 0920-654X</identifier><identifier>EISSN: 1573-4951</identifier><identifier>DOI: 10.1007/s10822-014-9803-6</identifier><identifier>PMID: 25323391</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Amino Acid Sequence ; Animal Anatomy ; Biodegradation ; Bundling ; Calorimetry, Differential Scanning ; Chemical engineering ; Chemistry ; Chemistry and Materials Science ; Circular Dichroism ; Computer Applications in Chemistry ; Computer simulation ; Contaminants ; Design engineering ; E coli ; High temperature ; Histology ; Hydrophobic and Hydrophilic Interactions ; Industrial products ; Melting point ; Microorganisms ; Molecular Dynamics Simulation ; Molecular Sequence Data ; Morphology ; Mutation ; Mutations ; Phase transitions ; Physical Chemistry ; Protein Conformation ; Protein Denaturation ; Protein Engineering - methods ; Protein Stability ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Stability ; Structural Homology, Protein ; Surface-Active Agents - chemistry ; Surfactants ; Systems stability ; Thermal stability ; Tolerances</subject><ispartof>Journal of computer-aided molecular design, 2015, Vol.29 (1), p.47-58</ispartof><rights>Springer International Publishing Switzerland 2014</rights><rights>Springer International Publishing Switzerland 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-dd17a331cdc55f4de6178d38a788151a7019bb0b5bb105abd757394554ad1d4f3</citedby><cites>FETCH-LOGICAL-c405t-dd17a331cdc55f4de6178d38a788151a7019bb0b5bb105abd757394554ad1d4f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10822-014-9803-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10822-014-9803-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25323391$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schaller, Andrea</creatorcontrib><creatorcontrib>Connors, Natalie K.</creatorcontrib><creatorcontrib>Dwyer, Mirjana Dimitrijev</creatorcontrib><creatorcontrib>Oelmeier, Stefan A.</creatorcontrib><creatorcontrib>Hubbuch, Jürgen</creatorcontrib><creatorcontrib>Middelberg, Anton P. J.</creatorcontrib><title>Computational study of elements of stability of a four-helix bundle protein biosurfactant</title><title>Journal of computer-aided molecular design</title><addtitle>J Comput Aided Mol Des</addtitle><addtitle>J Comput Aided Mol Des</addtitle><description>Biosurfactants are surface-active molecules produced principally by microorganisms. They are a sustainable alternative to chemically-synthesized surfactants, having the advantages of being non-toxic, highly functional, eco-friendly and biodegradable. However they are currently only used in a few industrial products due to costs associated with production and purification, which exceed those for commodity chemical surfactants. DAMP4, a member of a four-helix bundle biosurfactant protein family, can be produced in soluble form and at high yield in
Escherichia coli
, and can be recovered using a facile thermal phase-separation approach. As such, it encompasses an interesting synergy of biomolecular and chemical engineering with prospects for low-cost production even for industrial sectors. DAMP4 is highly functional, and due to its extraordinary thermal stability it can be purified in a simple two-step process, in which the combination of high temperature and salt leads to denaturation of all contaminants, whereas DAMP4 stays stable in solution and can be recovered by filtration. This study aimed to characterize and understand the fundamental drivers of DAMP4 stability to guide further process and surfactant design studies. The complementary use of experiments and molecular dynamics simulation revealed a broad pH and temperature tolerance for DAMP4, with a melting point of 122.4 °C, suggesting the hydrophobic core as the major contributor to thermal stability. Simulation of systematically created in silico variants of DAMP4 showed an influence of number and location of hydrophilic mutations in the hydrophobic core on stability, demonstrating a tolerance of up to three mutations before a strong loss in stability occurred. The results suggest a consideration of a balance of stability, functionality and kinetics for new designs according to their application, aiming for maximal functionality but at adequate stability to allow for cost-efficient production using thermal phase separation approaches.</description><subject>Amino Acid Sequence</subject><subject>Animal Anatomy</subject><subject>Biodegradation</subject><subject>Bundling</subject><subject>Calorimetry, Differential Scanning</subject><subject>Chemical engineering</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Circular Dichroism</subject><subject>Computer Applications in Chemistry</subject><subject>Computer simulation</subject><subject>Contaminants</subject><subject>Design engineering</subject><subject>E coli</subject><subject>High temperature</subject><subject>Histology</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Industrial products</subject><subject>Melting point</subject><subject>Microorganisms</subject><subject>Molecular Dynamics Simulation</subject><subject>Molecular Sequence Data</subject><subject>Morphology</subject><subject>Mutation</subject><subject>Mutations</subject><subject>Phase transitions</subject><subject>Physical Chemistry</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Protein Engineering - methods</subject><subject>Protein Stability</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Stability</subject><subject>Structural Homology, Protein</subject><subject>Surface-Active Agents - chemistry</subject><subject>Surfactants</subject><subject>Systems stability</subject><subject>Thermal stability</subject><subject>Tolerances</subject><issn>0920-654X</issn><issn>1573-4951</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kEtLxDAUhYMozjj6A9xIwY2baG6TNM1SBl8guFHQVUiaVDv0MTYpOP_e1I4igqtcuOec3PMhdAzkHAgRFx5InqaYAMMyJxRnO2gOXFDMJIddNCcyJTjj7HmGDrxfkeiRGdlHs5TTlFIJc_Sy7Jr1EHSoulbXiQ-D3SRdmbjaNa4Nfpx90Kaqq_C10EnZDT1-c3X1kZihtbVL1n0XXNUmpur80Je6CLoNh2iv1LV3R9t3gZ6urx6Xt_j-4eZueXmPC0Z4wNaC0JRCYQvOS2ZdBiK3NNciz4GDFgSkMcRwY4BwbayIBSXjnGkLlpV0gc6m3HjF--B8UE3lC1fXunXd4BVkHBjPqRBRevpHuopdYu9RFa-REiLGBYJJVfSd970r1bqvGt1vFBA1clcTdxW5q5G7yqLnZJs8mMbZH8c36ChIJ4GPq_bV9b--_jf1E5pBjbE</recordid><startdate>2015</startdate><enddate>2015</enddate><creator>Schaller, Andrea</creator><creator>Connors, Natalie K.</creator><creator>Dwyer, Mirjana Dimitrijev</creator><creator>Oelmeier, Stefan A.</creator><creator>Hubbuch, Jürgen</creator><creator>Middelberg, Anton P. 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J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Computational study of elements of stability of a four-helix bundle protein biosurfactant</atitle><jtitle>Journal of computer-aided molecular design</jtitle><stitle>J Comput Aided Mol Des</stitle><addtitle>J Comput Aided Mol Des</addtitle><date>2015</date><risdate>2015</risdate><volume>29</volume><issue>1</issue><spage>47</spage><epage>58</epage><pages>47-58</pages><issn>0920-654X</issn><eissn>1573-4951</eissn><abstract>Biosurfactants are surface-active molecules produced principally by microorganisms. They are a sustainable alternative to chemically-synthesized surfactants, having the advantages of being non-toxic, highly functional, eco-friendly and biodegradable. However they are currently only used in a few industrial products due to costs associated with production and purification, which exceed those for commodity chemical surfactants. DAMP4, a member of a four-helix bundle biosurfactant protein family, can be produced in soluble form and at high yield in
Escherichia coli
, and can be recovered using a facile thermal phase-separation approach. As such, it encompasses an interesting synergy of biomolecular and chemical engineering with prospects for low-cost production even for industrial sectors. DAMP4 is highly functional, and due to its extraordinary thermal stability it can be purified in a simple two-step process, in which the combination of high temperature and salt leads to denaturation of all contaminants, whereas DAMP4 stays stable in solution and can be recovered by filtration. This study aimed to characterize and understand the fundamental drivers of DAMP4 stability to guide further process and surfactant design studies. The complementary use of experiments and molecular dynamics simulation revealed a broad pH and temperature tolerance for DAMP4, with a melting point of 122.4 °C, suggesting the hydrophobic core as the major contributor to thermal stability. Simulation of systematically created in silico variants of DAMP4 showed an influence of number and location of hydrophilic mutations in the hydrophobic core on stability, demonstrating a tolerance of up to three mutations before a strong loss in stability occurred. The results suggest a consideration of a balance of stability, functionality and kinetics for new designs according to their application, aiming for maximal functionality but at adequate stability to allow for cost-efficient production using thermal phase separation approaches.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>25323391</pmid><doi>10.1007/s10822-014-9803-6</doi><tpages>12</tpages></addata></record> |
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| ispartof | Journal of computer-aided molecular design, 2015, Vol.29 (1), p.47-58 |
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| subjects | Amino Acid Sequence Animal Anatomy Biodegradation Bundling Calorimetry, Differential Scanning Chemical engineering Chemistry Chemistry and Materials Science Circular Dichroism Computer Applications in Chemistry Computer simulation Contaminants Design engineering E coli High temperature Histology Hydrophobic and Hydrophilic Interactions Industrial products Melting point Microorganisms Molecular Dynamics Simulation Molecular Sequence Data Morphology Mutation Mutations Phase transitions Physical Chemistry Protein Conformation Protein Denaturation Protein Engineering - methods Protein Stability Proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism Stability Structural Homology, Protein Surface-Active Agents - chemistry Surfactants Systems stability Thermal stability Tolerances |
| title | Computational study of elements of stability of a four-helix bundle protein biosurfactant |
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