Linked Life Data

17619185

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

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pubmed-article:17619185pubmed:abstractTextCateslytin (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.lld:pubmed
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pubmed-article:17619185pubmed:articleTitleVariability in secondary structure of the antimicrobial peptide Cateslytin in powder, solution, DPC micelles and at the air-water interface.lld:pubmed
pubmed-article:17619185pubmed:affiliationUMR 5248 CBMN, CNRS-Université Bordeaux 1-ENITAB, IECB, 2 rue Robert Escarpit, 33607, Pessac, France.lld:pubmed
pubmed-article:17619185pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:17619185pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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