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

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

SUBMITTER: Rost U 

PROVIDER: S-EPMC6022121 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature