Pro-apoptotic bax-α1 synthesis and evidence for β-sheet to α-helix conformational change as triggered by negatively charged lipid mβembranes
2007 (English)In: Journal of Peptide Science, ISSN 1075-2617, Vol. 13, no 2, 100-106 p.Article in journal (Refereed) Published
Solid phase synthesis of Bax-α1, 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-α1 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.
Place, publisher, year, edition, pages
2007. Vol. 13, no 2, 100-106 p.
solid phase synthesis, TFA removal, 19F NMR, UV circular dichroism, electrostatic interaction, apoptotic peptides
IdentifiersURN: urn:nbn:se:umu:diva-12371DOI: doi:10.1002/psc.803OAI: oai:DiVA.org:umu-12371DiVA: diva2:152042