Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-4-23
pubmed:abstractText
Temporin A (TA) is a small, basic and highly hydrophobic peptide, isolated from the skin of the European red frog, Rana temporaria. The TA (FLPLIGRVLSGIL-NH2) displays a broad spectrum of anti-microbial activity against Gram-positive bacteria and fungi Candida albicans. In this study we investigate the solution structure of two TA retro-analogues, (6-1)(7-13)-TA (GILPLFRVLSGIL-NH2) and retro-TA (LIGSLVRGILPLF-NH2) by using nuclear magnetic resonance (NMR). The 3D solution structure of the analogues was established by using inter-proton distances and vicinal coupling constants in the Simulated Annealing (SA) calculations (XPLOR program). The NMR conformational studies show the existence of the helical structure in the middle part of the (6-1)(7-13)-TA peptide and an unordered structure of the retro-TA analogue under the D3-TFE/H2O (3:7, v/v) conditions. Our investigations have shown that the hydrophobic cluster at N-terminus with the Pro amino acid residue in position 3 or 4, the helical structure and the amphipathic character of the peptide are responsible for the anti-microbial activity of the TA analogues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1075-2617
pubmed:author
pubmed:copyrightInfo
Copyright (c) 2007 European Peptide Society and John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
327-33
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Conformational solution studies of the anti-microbial temporin A retro-analogues by using NMR spectroscopy.
pubmed:affiliation
Faculty of Pharmacy, Medical University of Gda?sk, Gda?sk, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't