Drescher Simon, Meister Annette, Hause Gerd, Neuhaus Frederik, Balog Sandor, Brezesinski Gerald, Zumbuehl Andreas
Institute of Pharmacy-Biophysical Pharmacy, Martin Luther University (MLU) Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120 Halle (Saale), Germany.
Phospholipid Research Center, Im Neuenheimer Feld 515, 69120 Heidelberg, Germany.
Langmuir. 2020 Jul 28;36(29):8610-8616. doi: 10.1021/acs.langmuir.0c01522. Epub 2020 Jul 15.
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.
在生物膜中，蛋白质需要特定长度和链饱和度的独特脂质围绕。因此，对膜厚度的主动调节为膜蛋白的研究和操纵开辟了新的可能性。在这里，我们通过将1,3 - 二氨基磷脂与单链bola脂质混合，引入了不同程度叉指深度的订书磷脂概念。通过量热分析、电子显微镜、X射线和红外测量对混合膜进行了研究，以提供膜订书的完整生物物理特征。二氨基磷脂和bola脂质之间的匹配可以非常强，以至于完全诱导出一个比单个组分的凝胶相更稳定的新相。
