| pubmed-article:21308877 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C1136254 | lld:lifeskim |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:21308877 | lifeskim:mentions | umls-concept:C0018164 | lld:lifeskim |
| pubmed-article:21308877 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:21308877 | pubmed:dateCreated | 2011-2-10 | lld:pubmed |
| pubmed-article:21308877 | pubmed:abstractText | Gramicidin S (GS) is a cyclo-decapeptide antibiotic isolated from Bacillus brevis. The structural studies have shown that GS forms a two-stranded antiparallel ?-sheet imposed by two II' ?-turns. Despite its wide Gram+ and Gram- antimicrobial spectrum, GS is useless in therapy because of its high hemotoxicity in humans. It was found, however, that the analogues of GS-14 (GS with 14 amino acid residues) attained a better antimicrobial selectivity when their amphipatic moments were perturbed. In this study, we report effects of similar perturbations imposed on GS cyclo-decapeptide analogues. Having solved their structures by NMR/molecular dynamics and having tested their activities/selectivities, we have concluded that the idea of perturbation of the amphipatic moment does not work for GS-10_0 analogues. An innovative approach to the synthesis of head-to-tail cyclopeptides was used. | lld:pubmed |
| pubmed-article:21308877 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21308877 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21308877 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21308877 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21308877 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21308877 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21308877 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:21308877 | pubmed:issn | 1099-1387 | lld:pubmed |
| pubmed-article:21308877 | pubmed:author | pubmed-author:KamyszWojciec... | lld:pubmed |
| pubmed-article:21308877 | pubmed:author | pubmed-author:Rodziewicz-Mo... | lld:pubmed |
| pubmed-article:21308877 | pubmed:author | pubmed-author:CiarkowskiJer... | lld:pubmed |
| pubmed-article:21308877 | pubmed:author | pubmed-author:MickiewiczBea... | lld:pubmed |
| pubmed-article:21308877 | pubmed:author | pubmed-author:KamyszEl?biet... | lld:pubmed |
| pubmed-article:21308877 | pubmed:author | pubmed-author:Bieli?skaSylw... | lld:pubmed |
| pubmed-article:21308877 | pubmed:copyrightInfo | Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd. | lld:pubmed |
| pubmed-article:21308877 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21308877 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:21308877 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21308877 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21308877 | pubmed:pagination | 211-7 | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:meshHeading | pubmed-meshheading:21308877... | lld:pubmed |
| pubmed-article:21308877 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21308877 | pubmed:articleTitle | Synthesis, biological activity and solution structure of new analogues of the antimicrobial Gramicidin S. | lld:pubmed |
| pubmed-article:21308877 | pubmed:affiliation | University of Gda?sk, Faculty of Chemistry, Sobieskiego 18, Gda?sk, 80-952, Poland. kamysz@chem.univ.gda.pl | lld:pubmed |
| pubmed-article:21308877 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21308877 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
