Source:http://linkedlifedata.com/resource/pubmed/id/17585874
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2007-7-3
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pubmed:databankReference | |
pubmed:abstractText |
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 beta-hairpin, formed by two antiparallel beta-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the beta-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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author |
pubmed-author:ArsenievAlexander SAS,
pubmed-author:BalandinSergey VSV,
pubmed-author:FinkinaEkaterina IEI,
pubmed-author:KokryakovVladimir NVN,
pubmed-author:KudelinaIrina AIA,
pubmed-author:NadezhdinKirill DKD,
pubmed-author:OvchinnikovaTatiana VTV,
pubmed-author:ShenkarevZakhar OZO,
pubmed-author:ZhmakMaxim NMN
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
360
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
156-62
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pubmed:meshHeading |
pubmed-meshheading:17585874-Amino Acid Sequence,
pubmed-meshheading:17585874-Animals,
pubmed-meshheading:17585874-Computer Simulation,
pubmed-meshheading:17585874-Models, Chemical,
pubmed-meshheading:17585874-Models, Molecular,
pubmed-meshheading:17585874-Molecular Sequence Data,
pubmed-meshheading:17585874-Peptides,
pubmed-meshheading:17585874-Polychaeta,
pubmed-meshheading:17585874-Protein Conformation,
pubmed-meshheading:17585874-Recombinant Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Recombinant expression, synthesis, purification, and solution structure of arenicin.
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pubmed:affiliation |
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, 117997 Moscow, Russia. ovch@ibch.ru
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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