Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin
Differential precipitation of human plasma by ethanol is one of the most important processes for purifying therapeutic proteins, including human serum albumin. Better understanding of the effects of ethanol on the structure and stability of proteins is critical for effective and safe application of...
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| Veröffentlicht in: | International journal of biological macromolecules 2012-06, Vol.50 (5), p.1286-1291 |
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| container_title | International journal of biological macromolecules |
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| creator | Yoshikawa, Hiroki Hirano, Atsushi Arakawa, Tsutomu Shiraki, Kentaro |
| description | Differential precipitation of human plasma by ethanol is one of the most important processes for purifying therapeutic proteins, including human serum albumin. Better understanding of the effects of ethanol on the structure and stability of proteins is critical for effective and safe application of ethanol-induced protein precipitation. Here, we examined the effects of ethanol on the structure and solubility of bovine serum albumin (BSA) and SH-modified BSA. Ethanol caused BSA denaturation in a bimodal fashion, i.e., reduction of α-helix at low concentration and subsequent induction of the α-helical structure at higher concentration. In contrast, the solubility of BSA decreased monotonically. The secondary structure of SH-modified BSA was different from that of native BSA. Ethanol resulted in enhanced secondary structures of SH-modified BSA and decreased solubility monotonically. These results suggest the favorable interaction of ethanol with hydrophobic residues, leading to protein denaturation, but the unfavorable interaction with charged residues, leading to a reduction of protein solubility. |
| doi_str_mv | 10.1016/j.ijbiomac.2012.03.014 |
| format | Article |
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Better understanding of the effects of ethanol on the structure and stability of proteins is critical for effective and safe application of ethanol-induced protein precipitation. Here, we examined the effects of ethanol on the structure and solubility of bovine serum albumin (BSA) and SH-modified BSA. Ethanol caused BSA denaturation in a bimodal fashion, i.e., reduction of α-helix at low concentration and subsequent induction of the α-helical structure at higher concentration. In contrast, the solubility of BSA decreased monotonically. The secondary structure of SH-modified BSA was different from that of native BSA. Ethanol resulted in enhanced secondary structures of SH-modified BSA and decreased solubility monotonically. These results suggest the favorable interaction of ethanol with hydrophobic residues, leading to protein denaturation, but the unfavorable interaction with charged residues, leading to a reduction of protein solubility.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2012.03.014</identifier><identifier>PMID: 22484442</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Alcohol precipitation ; Alcohols - chemistry ; Alcohols - pharmacology ; Animals ; biopharmaceuticals ; bovine serum albumin ; Cattle ; chemical precipitation ; Crystallization ; Denaturation ; Destabilization ; Disulfides - chemistry ; ethanol ; Ethanol - chemistry ; Ethanol - pharmacology ; human serum albumin ; Humans ; Hydrophobic interaction ; hydrophobicity ; Protein Conformation - drug effects ; Protein Denaturation - drug effects ; protein secondary structure ; protein solubility ; Serum Albumin, Bovine - chemistry ; SH-modification ; Solubility - drug effects ; Water - chemistry</subject><ispartof>International journal of biological macromolecules, 2012-06, Vol.50 (5), p.1286-1291</ispartof><rights>2012 Elsevier B.V.</rights><rights>Copyright © 2012 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-e36c4f4e2c653c2bb51b052e6e793a4db963d569b7bf78b27afc7e6c003eff1d3</citedby><cites>FETCH-LOGICAL-c458t-e36c4f4e2c653c2bb51b052e6e793a4db963d569b7bf78b27afc7e6c003eff1d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0141813012001110$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22484442$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yoshikawa, Hiroki</creatorcontrib><creatorcontrib>Hirano, Atsushi</creatorcontrib><creatorcontrib>Arakawa, Tsutomu</creatorcontrib><creatorcontrib>Shiraki, Kentaro</creatorcontrib><title>Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>Differential precipitation of human plasma by ethanol is one of the most important processes for purifying therapeutic proteins, including human serum albumin. Better understanding of the effects of ethanol on the structure and stability of proteins is critical for effective and safe application of ethanol-induced protein precipitation. Here, we examined the effects of ethanol on the structure and solubility of bovine serum albumin (BSA) and SH-modified BSA. Ethanol caused BSA denaturation in a bimodal fashion, i.e., reduction of α-helix at low concentration and subsequent induction of the α-helical structure at higher concentration. In contrast, the solubility of BSA decreased monotonically. The secondary structure of SH-modified BSA was different from that of native BSA. Ethanol resulted in enhanced secondary structures of SH-modified BSA and decreased solubility monotonically. These results suggest the favorable interaction of ethanol with hydrophobic residues, leading to protein denaturation, but the unfavorable interaction with charged residues, leading to a reduction of protein solubility.</description><subject>Alcohol precipitation</subject><subject>Alcohols - chemistry</subject><subject>Alcohols - pharmacology</subject><subject>Animals</subject><subject>biopharmaceuticals</subject><subject>bovine serum albumin</subject><subject>Cattle</subject><subject>chemical precipitation</subject><subject>Crystallization</subject><subject>Denaturation</subject><subject>Destabilization</subject><subject>Disulfides - chemistry</subject><subject>ethanol</subject><subject>Ethanol - chemistry</subject><subject>Ethanol - pharmacology</subject><subject>human serum albumin</subject><subject>Humans</subject><subject>Hydrophobic interaction</subject><subject>hydrophobicity</subject><subject>Protein Conformation - drug effects</subject><subject>Protein Denaturation - drug effects</subject><subject>protein secondary structure</subject><subject>protein solubility</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>SH-modification</subject><subject>Solubility - drug effects</subject><subject>Water - chemistry</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAURq0KRIe2f6FkySbBrzieHagqD6kSC-ja8uO6c0dJXOxkpP77epiWLStLn879bJ9LyDWjHaNMfdp3uHeYJus7ThnvqOgok2dkw_SwbSml4g3Z1IS1mgl6Tt6Xsq-p6pl-R845l1pKyTdkdxsj-KU0KTZ29GmXxibNzbKDpqRxdTji8tTYOTRlyatf1gxHdLYLHuBvHrCsY8QA7ZQCRoTQuHTAuRZAXqfa6tYJ50vyNtqxwNXLeUHuv97-vvne3v389uPmy13rZa-XFoTyMkrgXvXCc-d65mjPQcGwFVYGt1Ui9GrrBhcH7fhgox9A-fphiJEFcUE-nnofc_qzQlnMhMXDONoZ0lpMtddzKTRlFVUn1OdUSoZoHjNONj9V6Mgpszevls3RsqHCVKd18PrljtVNEP6NvWqtwIcTEG0y9iFjMfe_aoOqK-i1FroSn08EVBcHhGyKR5g9BMx1HyYk_N8rngGTN5xG</recordid><startdate>20120601</startdate><enddate>20120601</enddate><creator>Yoshikawa, Hiroki</creator><creator>Hirano, Atsushi</creator><creator>Arakawa, Tsutomu</creator><creator>Shiraki, Kentaro</creator><general>Elsevier B.V</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20120601</creationdate><title>Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin</title><author>Yoshikawa, Hiroki ; 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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Alcohol precipitation Alcohols - chemistry Alcohols - pharmacology Animals biopharmaceuticals bovine serum albumin Cattle chemical precipitation Crystallization Denaturation Destabilization Disulfides - chemistry ethanol Ethanol - chemistry Ethanol - pharmacology human serum albumin Humans Hydrophobic interaction hydrophobicity Protein Conformation - drug effects Protein Denaturation - drug effects protein secondary structure protein solubility Serum Albumin, Bovine - chemistry SH-modification Solubility - drug effects Water - chemistry |
| title | Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin |
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