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Pro‐apoptotic bax‐α1 synthesis and evidence for β‐sheet to α‐helix conformational change as triggered by negatively charged lipid membranes
Author(s) -
Sani MarcAntoine,
Loudet Cécile,
Gröbner Gerhard,
Dufourc Erick J.
Publication year - 2007
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.803
Subject(s) - circular dichroism , chemistry , membrane , peptide , random coil , conformational change , vesicle , protein secondary structure , helix (gastropod) , aqueous solution , biophysics , crystallography , stereochemistry , biochemistry , organic chemistry , biology , ecology , snail
Solid phase synthesis of Bax‐α1, the 25 amino acids domain ( 14 TSSEQIMKTGALLLQGFIQDRAGRM 38 ) 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 19 F‐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. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.