pubmed-article:17585874 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17585874 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:17585874 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:17585874 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:17585874 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
pubmed-article:17585874 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:17585874 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
pubmed-article:17585874 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:17585874 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:17585874 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:17585874 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:17585874 | pubmed:dateCreated | 2007-7-3 | lld:pubmed |
pubmed-article:17585874 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17585874 | 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. | lld:pubmed |
pubmed-article:17585874 | pubmed:language | eng | lld:pubmed |
pubmed-article:17585874 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17585874 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17585874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17585874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17585874 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17585874 | pubmed:month | Aug | lld:pubmed |
pubmed-article:17585874 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:17585874 | pubmed:author | pubmed-author:ArsenievAlexa... | lld:pubmed |
pubmed-article:17585874 | pubmed:author | pubmed-author:KokryakovVlad... | lld:pubmed |
pubmed-article:17585874 | pubmed:author | pubmed-author:KudelinaIrina... | lld:pubmed |
pubmed-article:17585874 | pubmed:author | pubmed-author:ZhmakMaxim... | lld:pubmed |
pubmed-article:17585874 | pubmed:author | pubmed-author:ShenkarevZakh... | lld:pubmed |
pubmed-article:17585874 | pubmed:author | pubmed-author:OvchinnikovaT... | lld:pubmed |
pubmed-article:17585874 | pubmed:author | pubmed-author:BalandinSerge... | lld:pubmed |
pubmed-article:17585874 | pubmed:author | pubmed-author:NadezhdinKiri... | lld:pubmed |
pubmed-article:17585874 | pubmed:author | pubmed-author:FinkinaEkater... | lld:pubmed |
pubmed-article:17585874 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17585874 | pubmed:day | 17 | lld:pubmed |
pubmed-article:17585874 | pubmed:volume | 360 | lld:pubmed |
pubmed-article:17585874 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17585874 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17585874 | pubmed:pagination | 156-62 | lld:pubmed |
pubmed-article:17585874 | pubmed:meshHeading | pubmed-meshheading:17585874... | lld:pubmed |
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pubmed-article:17585874 | pubmed:meshHeading | pubmed-meshheading:17585874... | lld:pubmed |
pubmed-article:17585874 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17585874 | pubmed:articleTitle | Recombinant expression, synthesis, purification, and solution structure of arenicin. | lld:pubmed |
pubmed-article:17585874 | pubmed:affiliation | Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, 117997 Moscow, Russia. ovch@ibch.ru | lld:pubmed |
pubmed-article:17585874 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17585874 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17585874 | lld:pubmed |