Variability in secondary structure of the antimicrobial peptide Cateslytin in powder, solution, DPC micelles and at the air¨Cwater interface
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- 作者：Frantz Jean-Fran?ois ; Lucie Khemt¨¦mourian ; Beno?t Odaert ; Sabine Castano ; Axelle Gr¨¦lard ; Claude Manigand ; Katell Bathany ; Marie-H¨¦l¨¨ne Metz-Boutigue and Erick J. Dufourc
- 关键词：Antimicrobial peptides ; Cateslytin ; Circular dichroism ; Solid phase synthesis ; MALDI ; TOF mass spectrometry ; Solution NMR
- 刊名：European Biophysics Journal
- 出版年：2007
- 出版时间：November, 2007
- 年：2007
- 卷：36
- 期：8
- 页码：1019-1027
- 全文大小：437 KB
文摘
Cateslytin (bCGA 344RSMRLSFRARGYGFR358), 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 α-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 β-sheet contribution of almost 100 % is detected at the air–water interface. Such conformational plasticity is discussed regarding the antimicrobial action of Cateslytin.