Synthesis and secondary structure in membranes of the Bcl-2 anti-apoptotic domain BH4
2006 (English)In: Journal of Peptide Science, ISSN 1075-2617, Vol. 12, 58-64 p.Article in journal (Refereed) Published
Solid phase synthesis of BH4, the 26 amino-acid domain (6RTGYDNREIVMKYIHYKLSQRGYEWD31) 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 15N-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 -sheeted structures in water that convert progressively into -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.
Place, publisher, year, edition, pages
2006. Vol. 12, 58-64 p.
solid phase synthesis, reverse-phase HPLC, MALDI-TOF mass spectrometry, circular dichroism, non-protected tryptophan, apoptotic peptides, 15N-labelled amino acids
IdentifiersURN: urn:nbn:se:umu:diva-12545DOI: doi:10.1002/psc.686OAI: oai:DiVA.org:umu-12545DiVA: diva2:152216