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

Babii, Oleg 1; Afonin, Sergii 2; Schober, Tim 1; Komarov, Igor V.; Ulrich, Anne S. 1,2
1 Institut für Organische Chemie (IOC), Karlsruher Institut für Technologie (KIT)
2 Institut für Biologische Grenzflächen (IBG), Karlsruher Institut für Technologie (KIT)


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 $^{19}$F-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. ... mehr

Verlagsausgabe §
DOI: 10.5445/IR/1000075872
Veröffentlicht am 02.03.2018
DOI: 10.1016/j.bbamem.2017.09.021
Zitationen: 8
Zitationen: 9
Cover der Publikation
Zugehörige Institution(en) am KIT Institut für Biologische Grenzflächen (IBG)
Institut für Organische Chemie (IOC)
Publikationstyp Zeitschriftenaufsatz
Publikationsjahr 2017
Sprache Englisch
Identifikator ISSN: 0005-2736, 1879-2642
KITopen-ID: 1000075872
HGF-Programm 47.02.02 (POF III, LK 01) Zellpopul.auf Biofunk.Oberflächen IBG-2
Erschienen in Biochimica et biophysica acta / Biomembranes
Verlag Elsevier
Band 1859
Heft 12
Seiten 2505-2515
Vorab online veröffentlicht am 27.09.2017
Schlagwörter Molecular flexibility/rigidity, Membrane-active peptides, Molecular photoswitches, Diarylethene, Differential scanning calorimetry, Solid-state 19F-NMR spectroscopy
Nachgewiesen in Dimensions
Web of Science
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