Journal article

Pro-apoptotic bax-alpha 1 synthesis and evidence for beta-sheet to alpha-helix conformational change as triggered by negatively charged lipid membranes

Marc-Antoine Sani, Cecile Loudet, Gerhard Grobner, Erick J Dufourc

JOURNAL OF PEPTIDE SCIENCE | JOHN WILEY & SONS LTD | Published : 2007

Abstract

Solid phase synthesis of Bax-alpha1, the 25 amino acids domain (14TSSEQIMKTGALLLQGFIQDRAGRM38) of the pro-apoptotic 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-alpha1 is present as a mixture of beta-sheet and unstructured (random coil) conformations. A marked change from beta-sheet to alpha-helix secondary structures is observed upon interaction with ..

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