Tuning the Thickness of a Biomembrane by Stapling Diamidophospholipids with Bolalipids

In a biological membrane, proteins require specific lipids of distinctive length and chain saturation surrounding them. The active tuning of the membrane thickness therefore opens new possibilities in the study and manipulation of membrane proteins. Here, we introduce the concept of stapling phospho...

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Veröffentlicht in:Langmuir 2020-07, Vol.36 (29), p.8610-8616
Hauptverfasser: Drescher, Simon, Meister, Annette, Hause, Gerd, Neuhaus, Frederik, Balog, Sandor, Brezesinski, Gerald, Zumbuehl, Andreas
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container_end_page 8616
container_issue 29
container_start_page 8610
container_title Langmuir
container_volume 36
creator Drescher, Simon
Meister, Annette
Hause, Gerd
Neuhaus, Frederik
Balog, Sandor
Brezesinski, Gerald
Zumbuehl, Andreas
description In a biological membrane, proteins require specific lipids of distinctive length and chain saturation surrounding them. The active tuning of the membrane thickness therefore opens new possibilities in the study and manipulation of membrane proteins. Here, we introduce the concept of stapling phospholipids to different degrees of interdigitation depth by mixing 1,3-diamidophospholipids with single-chain bolalipids. The mixed membranes were studied by calorimetric assays, electron microscopy, X-ray, and infrared measurements to provide a complete biophysical characterization of membrane stapling. The matching between the diamidophospholipids and the bolalipids can be so strong as to completely induce a new phase that is more stable than the gel phase of the individual components.
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