Synthesis and secondary structure in membranes of the Bcl-2 anti-apoptotic domain BH4

✍ Scribed by Lucie Khemtémourian; Marc-Antoine Sani; Katell Bathany; Gerhard Gröbner; Erick J. Dufourc

• Book ID: 105360504
• Publisher: John Wiley and Sons
• Year: 2005
• Tongue: English
• Weight: 294 KB
• Volume: 12
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.686

✦ Synopsis

Abstract

Solid phase synthesis of BH4, the 26 amino‐acid domain (^6^RTGYDNREIVMKYIHYKLSQRGYEWD^31^) of the anti‐apoptotic Bcl‐2 protein has been accomplished using Fmoc chemistry. The use of peculiar cleavage conditions provided high yields after purification such that tens to hundreds of mg could be obtained. A ^15^N‐labelled version of the peptide could also be synthesized for NMR studies in membranes. The peptide purity was not lower than 98% as controlled by UV and MALDI‐TOF mass spectrometry. The secondary structure was determined in water, trifluoroethanol (TFE) and in lipid membrane using UV circular dichroism. The peptide shows dominant β‐sheeted structures in water that convert progressively into α‐helical features upon addition of TFE or membrane. The amphipathic character of the helix suggests that the peptide might have a structure akin to those of antimicrobial peptides upon interaction with membranes. Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd.