| pubmed-article:20074208 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20074208 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:20074208 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:20074208 | lifeskim:mentions | umls-concept:C1136254 | lld:lifeskim |
| pubmed-article:20074208 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:20074208 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:20074208 | lifeskim:mentions | umls-concept:C0300260 | lld:lifeskim |
| pubmed-article:20074208 | lifeskim:mentions | umls-concept:C0205254 | lld:lifeskim |
| pubmed-article:20074208 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:20074208 | pubmed:dateCreated | 2010-2-9 | lld:pubmed |
| pubmed-article:20074208 | pubmed:abstractText | The natural antimicrobial cationic peptide protegrin-1 displays a broad spectrum of antimicrobial activity and rapidly kills pathogens by interacting with their cell membrane. We investigated the structure-activity relationships of three protegrin-1 analogues: IB-367 (RGGLCYCRGRFCVCVGR-NH(2)), BM-1 (RGLCYCRGRFCVCVG-NH(2)) and BM-2 (RGLCYRPRFVCVG-NH(2)). Our antimicrobial and antifungal activity studies of these peptides showed that BM-1 was much more active than IB-367 against Gram-positive bacteria and fungi, whereas BM-2 was inactive. The BM-1 peptide showed fourfold reduced haemolysis relative to IB-367, an additional advantage of this peptide. In addition, BM-1 was about 15% cheaper than IB-367 to synthesize. The absence of two cysteine residues in the BM-2 sequence could be the main reason for its unstable conformation and antimicrobial inactivity. The solution structures of these peptides were determined in dimethyl sulphoxide using two-dimensional NMR and restrained molecular dynamics calculations. IB-367 and BM-1 formed short, antiparallel, beta-hairpin structures connected by a type II' beta-turn. The shorter, inactive BM-2 analogue exhibited major and minor conformations (predominantly unordered) in the NMR spectra and was much more flexible. | lld:pubmed |
| pubmed-article:20074208 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20074208 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074208 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20074208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074208 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20074208 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:20074208 | pubmed:issn | 1742-4658 | lld:pubmed |
| pubmed-article:20074208 | pubmed:author | pubmed-author:KamyszWojciec... | lld:pubmed |
| pubmed-article:20074208 | pubmed:author | pubmed-author:Rodziewicz-Mo... | lld:pubmed |
| pubmed-article:20074208 | pubmed:author | pubmed-author:SikorskaEmili... | lld:pubmed |
| pubmed-article:20074208 | pubmed:author | pubmed-author:MickiewiczBea... | lld:pubmed |
| pubmed-article:20074208 | pubmed:author | pubmed-author:GreberKatarzy... | lld:pubmed |
| pubmed-article:20074208 | pubmed:author | pubmed-author:KamyszElzbiet... | lld:pubmed |
| pubmed-article:20074208 | pubmed:author | pubmed-author:SzultkaLukasz... | lld:pubmed |
| pubmed-article:20074208 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20074208 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:20074208 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20074208 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20074208 | pubmed:pagination | 1010-22 | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:meshHeading | pubmed-meshheading:20074208... | lld:pubmed |
| pubmed-article:20074208 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20074208 | pubmed:articleTitle | Antimicrobial and conformational studies of the active and inactive analogues of the protegrin-1 peptide. | lld:pubmed |
| pubmed-article:20074208 | pubmed:affiliation | Faculty of Chemistry, University of Gda?sk, Poland. | lld:pubmed |
| pubmed-article:20074208 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20074208 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20074208 | lld:pubmed |
