Pro-apoptotic bax-α1 synthesis and evidence for β-sheet to α-helix conformational change as triggered by negatively charged lipid membranes - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Peptide Science Année : 2007

Pro-apoptotic bax-α1 synthesis and evidence for β-sheet to α-helix conformational change as triggered by negatively charged lipid membranes

Résumé

Solid phase synthesis of Bax-α 1, the 25 amino acids domain (14TSSEQIMKTGALLLQGFIQDRAGRM38) of the proapoptotic Bax protein has been accomplished using Fmoc chemistry. A new fast and harmless protocol is described for complete TFA removal from the purified peptide powder leading to a final purity greater than 98% as controlled by 19F-NMR, UV and MALDI-TOF mass spectrometry. Secondary structure was determined in various solution and membrane media using UV Circular Dichroism. In water solution, Bax-α 1 is present as a mixture of β-sheet and unstructured (random coil) conformations. A marked change from β-sheet to α-helix secondary structures is observed upon interaction with negatively charged phospholipids vesicles whereas neutral lipid membranes have no significant effect on the aqueous peptide conformation. Results are discussed in terms of Bax binding to mitochondrial membranes. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.

Dates et versions

hal-01564160 , version 1 (18-07-2017)

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M.-A. Sani, C. Loudet, G. Gröbner, E.J. Dufourc. Pro-apoptotic bax-α1 synthesis and evidence for β-sheet to α-helix conformational change as triggered by negatively charged lipid membranes. Journal of Peptide Science, 2007, 13 (2), pp.100-106. ⟨10.1002/psc.803⟩. ⟨hal-01564160⟩

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