Linked Life Data

17619185

Source:http://linkedlifedata.com/resource/pubmed/id/17619185

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2007-10-31
pubmed:abstractText
Cateslytin (bCGA (344)RSMRLSFRARGYGFR(358)), a five positively charged 15 amino-acid residues arginine-rich antimicrobial peptide, was synthesized using a very efficient procedure leading to high yields and to a 99% purity as determined by HPLC and mass spectrometry. Circular dichroism, polarized attenuated total reflectance fourier transformed infrared, polarization modulation infrared reflection Absorption spectroscopies and proton two-dimensional NMR revealed the flexibility of such a peptide. Whereas being mostly disordered as a dry powder or in water solution, the peptide acquires a alpha-helical character in the "membrane mimicking" solvent trifuoroethanol. In zwitterionic micelles of dodecylphophatidylcholine the helical character is retained but to a lesser extent, the peptide returning mainly to its disordered state. A beta-sheet contribution of almost 100% is detected at the air-water interface. Such conformational plasticity is discussed regarding the antimicrobial action of Cateslytin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0175-7571
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1019-27
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Variability in secondary structure of the antimicrobial peptide Cateslytin in powder, solution, DPC micelles and at the air-water interface.
pubmed:affiliation
UMR 5248 CBMN, CNRS-Université Bordeaux 1-ENITAB, IECB, 2 rue Robert Escarpit, 33607, Pessac, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't