NDLI: β-Glutamine-mediated self-association of transmembrane β-peptides within lipid bilayers

Content Provider	Royal Society of Chemistry (RSC)
Author	Rost, U. Steinem, C. Diederichsen, U.
Copyright Year	2016
Abstract	Transmembrane β-peptide helices and their association in lipid membranes are still widely unexplored. We designed and synthesized transmembrane β-peptides harboring different numbers of D-β3-glutamine residues (hGln) by solid phase peptide synthesis. By means of circular dichroism spectroscopic measurements, the secondary structure of the β-peptides reconstituted into unilamellar vesicles was determined to be similar to a right-handed 314-helix. Fluorescence spectroscopy using D-β3-tryptophan residues strongly suggested a transmembrane orientation. Two or three hGln served as recognition units between the helices to allow helix–helix assembly driven by hydrogen bond formation. The association state of the transmembrane β-peptides as a function of the number of hGln residues was investigated by fluorescence resonance energy transfer (FRET). Therefore, two fluorescence probes (NBD, TAMRA) were covalently attached to the side chains of the transmembrane β-peptide helices. The results clearly demonstrate that only β-peptides with hGln as recognition units assemble into oligomers, presumably trimers. Temperature dependent FRET experiments further show that the strength of the helix–helix association is a function of the number of hGln residues in the helix.
Starting Page	5900
Ending Page	5907
Page Count	8
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	7
Issue Number	9
Journal	Chemical Science
DOI	10.1039/c6sc01147k
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Fluorescence spectroscopy Beta-peptide Förster resonance energy transfer Tryptophan Peptide synthesis Biomolecular structure Lipid Glutamine Circular dichroism Hydrogen bond
Content Type	Text
Resource Type	Article
Subject	Chemistry

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