Source:http://linkedlifedata.com/resource/pubmed/id/17285588
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2007-4-23
|
pubmed:abstractText |
Arenicin-1 (AR-1) is a novel antimicrobial peptide that was isolated from coelomocytes of the marine polychaeta lugworm Arenicola marina and shown to contain a single disulfide bond between Cys3 and Cys20, forming an 18-residue ring [Ovchinnikova, T. V. et al., FEBS Lett 2004, 577, 209-214]. To determine the role of this disulfide bond, we synthesized AR-1 (RWCVYAYVRVRGVLVRYRRCW) and its linear derivative, arenicin-1-S (AR-1-S: RWSVYAYVRVRGVLVRYRRSW). Activity assays revealed that AR-1-S is somewhat less active against bacterial cells than AR-1. Both peptides were very hydrophobic, and displayed cytotoxicity against human red blood cells. Analysis of the tertiary structures of AR-1 and AR-1-S by NMR spectroscopy disclosed that AR-1 has two-stranded antiparallel beta-sheet structures with amphipathicity, while AR-1-S displays a random coil structure in DMSO. Our biological data for AR-1 and AR-1-S indicate that the hydrophobic-hydrophilic balance, disulfide bridge, and the amphipathic beta-sheet structure of the peptides play important roles in their biological activities. Elucidation of the structure of AR-1 and its derivative should facilitate the design of novel non-cytotoxic peptide antibiotics with potent antibacterial activities.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/arenicin-1, Arenicola marina
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0006-3525
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
88
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
208-16
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:17285588-Amino Acid Sequence,
pubmed-meshheading:17285588-Anti-Bacterial Agents,
pubmed-meshheading:17285588-Antimicrobial Cationic Peptides,
pubmed-meshheading:17285588-Bacteria,
pubmed-meshheading:17285588-Helminth Proteins,
pubmed-meshheading:17285588-Hemolysis,
pubmed-meshheading:17285588-Humans,
pubmed-meshheading:17285588-Models, Molecular,
pubmed-meshheading:17285588-Molecular Sequence Data,
pubmed-meshheading:17285588-Molecular Structure,
pubmed-meshheading:17285588-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17285588-Peptides
|
pubmed:year |
2007
|
pubmed:articleTitle |
Solution structures and biological functions of the antimicrobial peptide, arenicin-1, and its linear derivative.
|
pubmed:affiliation |
Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, IBST, Konkuk University, Seoul, Korea.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|