Recombinant expression, synthesis, purification, and solution structure of arenicin
Arenicins are 21-residue cationic antimicrobial peptides, isolated from marine polychaeta Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in Escherichia coli. Both arenicin isoforms were sy...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2007-08, Vol.360 (1), p.156-162 |
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| creator | Ovchinnikova, Tatiana V. Shenkarev, Zakhar O. Nadezhdin, Kirill D. Balandin, Sergey V. Zhmak, Maxim N. Kudelina, Irina A. Finkina, Ekaterina I. Kokryakov, Vladimir N. Arseniev, Alexander S. |
| description | Arenicins are 21-residue cationic antimicrobial peptides, isolated from marine polychaeta
Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in
Escherichia coli. Both arenicin isoforms were synthesized using the Fmoc-based solid-phase strategy. Recombinant and synthetic arenicins were purified, and their antimicrobial and spectroscopic properties were analyzed. NMR investigation shows that in water solution arenicin-2 displays a prolonged β-hairpin, formed by two antiparallel β-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the β-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon binding. Arenicin strongly binds to anionic lipid (POPE/POPG) vesicles in contrast with zwitterionic (POPC) ones. These results suggest that arenicins are membrane active peptides and point to possible mechanism of their selectivity toward bacterial cells. |
| doi_str_mv | 10.1016/j.bbrc.2007.06.029 |
| format | Article |
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Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in
Escherichia coli. Both arenicin isoforms were synthesized using the Fmoc-based solid-phase strategy. Recombinant and synthetic arenicins were purified, and their antimicrobial and spectroscopic properties were analyzed. NMR investigation shows that in water solution arenicin-2 displays a prolonged β-hairpin, formed by two antiparallel β-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the β-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon binding. Arenicin strongly binds to anionic lipid (POPE/POPG) vesicles in contrast with zwitterionic (POPC) ones. These results suggest that arenicins are membrane active peptides and point to possible mechanism of their selectivity toward bacterial cells.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2007.06.029</identifier><identifier>PMID: 17585874</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Antimicrobial activity ; Antimicrobial peptide ; Arenicin ; Arenicola marina ; Computer Simulation ; Escherichia coli ; Expression ; Folding ; Fusion protein ; Lugworm ; Marine invertebrate ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; NMR ; Peptides - chemistry ; Peptides - genetics ; Peptides - isolation & purification ; Peptides - metabolism ; Polychaeta ; Polychaeta - metabolism ; Protein Conformation ; Purification ; Recombinant ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - ultrastructure ; β-Hairpin</subject><ispartof>Biochemical and biophysical research communications, 2007-08, Vol.360 (1), p.156-162</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-2f6a5c2af189fc7307476fa0bb02c2c40264d932fc59dfd77e6f12f524e7844f3</citedby><cites>FETCH-LOGICAL-c451t-2f6a5c2af189fc7307476fa0bb02c2c40264d932fc59dfd77e6f12f524e7844f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X07012454$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17585874$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ovchinnikova, Tatiana V.</creatorcontrib><creatorcontrib>Shenkarev, Zakhar O.</creatorcontrib><creatorcontrib>Nadezhdin, Kirill D.</creatorcontrib><creatorcontrib>Balandin, Sergey V.</creatorcontrib><creatorcontrib>Zhmak, Maxim N.</creatorcontrib><creatorcontrib>Kudelina, Irina A.</creatorcontrib><creatorcontrib>Finkina, Ekaterina I.</creatorcontrib><creatorcontrib>Kokryakov, Vladimir N.</creatorcontrib><creatorcontrib>Arseniev, Alexander S.</creatorcontrib><title>Recombinant expression, synthesis, purification, and solution structure of arenicin</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Arenicins are 21-residue cationic antimicrobial peptides, isolated from marine polychaeta
Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in
Escherichia coli. Both arenicin isoforms were synthesized using the Fmoc-based solid-phase strategy. Recombinant and synthetic arenicins were purified, and their antimicrobial and spectroscopic properties were analyzed. NMR investigation shows that in water solution arenicin-2 displays a prolonged β-hairpin, formed by two antiparallel β-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the β-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon binding. Arenicin strongly binds to anionic lipid (POPE/POPG) vesicles in contrast with zwitterionic (POPC) ones. These results suggest that arenicins are membrane active peptides and point to possible mechanism of their selectivity toward bacterial cells.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antimicrobial activity</subject><subject>Antimicrobial peptide</subject><subject>Arenicin</subject><subject>Arenicola marina</subject><subject>Computer Simulation</subject><subject>Escherichia coli</subject><subject>Expression</subject><subject>Folding</subject><subject>Fusion protein</subject><subject>Lugworm</subject><subject>Marine invertebrate</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>NMR</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptides - isolation & purification</subject><subject>Peptides - metabolism</subject><subject>Polychaeta</subject><subject>Polychaeta - metabolism</subject><subject>Protein Conformation</subject><subject>Purification</subject><subject>Recombinant</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - ultrastructure</subject><subject>β-Hairpin</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLAzEUhYMotj7-gAuZlavOeJNmkgm4keILBMEHuAuZzA2mtJmazIj-e6e24E5Xl8P9zll8hJxQKChQcT4v6jraggHIAkQBTO2QMQUFOaPAd8kYAETOFH0dkYOU5gCUcqH2yYjKsiorycfk6RFtu6x9MKHL8HMVMSXfhkmWvkL3hsmnSbbqo3femu7nYUKTpXbRr1OWutjbro-YtS4zEYO3PhyRPWcWCY-395C8XF89z27z-4ebu9nlfW55SbucOWFKy4yjlXJWTkFyKZyBugZmmeXABG_UlDlbqsY1UqJwlLmScZQV5256SM42u6vYvveYOr30yeJiYQK2fdIShOCM0X9BqqQqp6waQLYBbWxTiuj0KvqliV-agl4713O9dq7XzjUIPTgfSqfb9b5eYvNb2UoegIsNgIOMD49RJ-sxWGx8RNvppvV_7X8DpRGTqg</recordid><startdate>20070817</startdate><enddate>20070817</enddate><creator>Ovchinnikova, Tatiana V.</creator><creator>Shenkarev, Zakhar O.</creator><creator>Nadezhdin, Kirill D.</creator><creator>Balandin, Sergey V.</creator><creator>Zhmak, Maxim N.</creator><creator>Kudelina, Irina A.</creator><creator>Finkina, Ekaterina I.</creator><creator>Kokryakov, Vladimir N.</creator><creator>Arseniev, Alexander S.</creator><general>Elsevier Inc</general><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20070817</creationdate><title>Recombinant expression, synthesis, purification, and solution structure of arenicin</title><author>Ovchinnikova, Tatiana V. ; Shenkarev, Zakhar O. ; Nadezhdin, Kirill D. ; Balandin, Sergey V. ; Zhmak, Maxim N. ; Kudelina, Irina A. ; Finkina, Ekaterina I. ; Kokryakov, Vladimir N. ; Arseniev, Alexander S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-2f6a5c2af189fc7307476fa0bb02c2c40264d932fc59dfd77e6f12f524e7844f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antimicrobial activity</topic><topic>Antimicrobial peptide</topic><topic>Arenicin</topic><topic>Arenicola marina</topic><topic>Computer Simulation</topic><topic>Escherichia coli</topic><topic>Expression</topic><topic>Folding</topic><topic>Fusion protein</topic><topic>Lugworm</topic><topic>Marine invertebrate</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>NMR</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>Peptides - isolation & purification</topic><topic>Peptides - metabolism</topic><topic>Polychaeta</topic><topic>Polychaeta - metabolism</topic><topic>Protein Conformation</topic><topic>Purification</topic><topic>Recombinant</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - ultrastructure</topic><topic>β-Hairpin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ovchinnikova, Tatiana V.</creatorcontrib><creatorcontrib>Shenkarev, Zakhar O.</creatorcontrib><creatorcontrib>Nadezhdin, Kirill D.</creatorcontrib><creatorcontrib>Balandin, Sergey V.</creatorcontrib><creatorcontrib>Zhmak, Maxim N.</creatorcontrib><creatorcontrib>Kudelina, Irina A.</creatorcontrib><creatorcontrib>Finkina, Ekaterina I.</creatorcontrib><creatorcontrib>Kokryakov, Vladimir N.</creatorcontrib><creatorcontrib>Arseniev, Alexander S.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ovchinnikova, Tatiana V.</au><au>Shenkarev, Zakhar O.</au><au>Nadezhdin, Kirill D.</au><au>Balandin, Sergey V.</au><au>Zhmak, Maxim N.</au><au>Kudelina, Irina A.</au><au>Finkina, Ekaterina I.</au><au>Kokryakov, Vladimir N.</au><au>Arseniev, Alexander S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recombinant expression, synthesis, purification, and solution structure of arenicin</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2007-08-17</date><risdate>2007</risdate><volume>360</volume><issue>1</issue><spage>156</spage><epage>162</epage><pages>156-162</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Arenicins are 21-residue cationic antimicrobial peptides, isolated from marine polychaeta
Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in
Escherichia coli. Both arenicin isoforms were synthesized using the Fmoc-based solid-phase strategy. Recombinant and synthetic arenicins were purified, and their antimicrobial and spectroscopic properties were analyzed. NMR investigation shows that in water solution arenicin-2 displays a prolonged β-hairpin, formed by two antiparallel β-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the β-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon binding. Arenicin strongly binds to anionic lipid (POPE/POPG) vesicles in contrast with zwitterionic (POPC) ones. These results suggest that arenicins are membrane active peptides and point to possible mechanism of their selectivity toward bacterial cells.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17585874</pmid><doi>10.1016/j.bbrc.2007.06.029</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Antimicrobial activity Antimicrobial peptide Arenicin Arenicola marina Computer Simulation Escherichia coli Expression Folding Fusion protein Lugworm Marine invertebrate Models, Chemical Models, Molecular Molecular Sequence Data NMR Peptides - chemistry Peptides - genetics Peptides - isolation & purification Peptides - metabolism Polychaeta Polychaeta - metabolism Protein Conformation Purification Recombinant Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - ultrastructure β-Hairpin |
| title | Recombinant expression, synthesis, purification, and solution structure of arenicin |
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