Details

Autor(en) / Beteiligte

• Babii, Oleg
• Afonin, Sergii
• Schober, Tim
• Komarov, Igor V.
• Ulrich, Anne S.

Titel

Flexibility vs rigidity of amphipathic peptide conjugates when interacting with lipid bilayers

Ist Teil von

• Biochimica et biophysica acta. Biomembranes, 2017-12, Vol.1859 (12), p.2505-2515

Ort / Verlag

Netherlands: Elsevier B.V

Erscheinungsjahr

2017

Quelle

MEDLINE

Beschreibungen/Notizen

• For the first time, the photoisomerization of a diarylethene moiety (DAET) in peptide conjugates was used to probe the effects of molecular rigidity/flexibility on the structure and behavior of model peptides bound to lipid membranes. The DAET unit was incorporated into the backbones of linear peptide-based constructs, connecting two amphipathic sequences (derived from the β-stranded peptide (KIGAKI)3 and/or the α-helical peptide BP100). A β-strand-DAET-α-helix and an α-helix-DAET-α-helix models were synthesized and studied in phospholipid membranes. Light-induced photoisomerization of the linker allowed the generation of two forms of each conjugate, which differed in the conformational mobility of the junction between the α-helical and/or the β-stranded part of these peptidomimetic molecules. A detailed study of their structural, orientational and conformational behavior, both in isotropic solution and in phospholipid model membranes, was carried out using circular dichroism and solid-state 19F-NMR spectroscopy. The study showed that the rigid and flexible forms of the two conjugates had appreciably different structures only when embedded in an anisotropic lipid environment and only in the gel phase. The influence of the rigidity/flexibility of the studied conjugates on the lipid thermotropic phase transition was also investigated by differential scanning calorimetry. Both models were found to destabilize the lamellar gel phases. [Display omitted] •DAET building blocks can be used to study rigidity/flexibility effects in supramolecular model systems.•Photoswitchable DAET linkers perturb only up to 3–4 adjacent amino acid residues.•Membrane-bound amphiphilic secondary structure elements exert a negligible influence on each other when linked by DAET.•The rigidity of peptide conjugates affected their structural behavior only in the lipid gel phase.