One of the main features of the cell membrane is its spatiotemporal control over domain architectures, which lead to the construct of supramolecular assemblies that perform specific functions.  Engineering lipid membranes to mimic this behavior could enable the creation of novel nanoscale systems for sequestration and transport, environmental sensing, hierarchical assembly, and the development of models for understanding budding and fission/fusion events.  In this presentation, our most recent efforts in the study and engineering of lipid membranes to selectively bind proteins to domains will be described. Previously, we've shown that domains functionalize with metal chelates (e.g., Cu(II)-IDA, Ni(II)-NTA) selectively bound his-tagged proteins with subsequent induction of membrane curvature localized to the domain.  Recently, we've explored the use of lipid structure and multivalent binding interactions to facilitate temporal control over domain formation.  Our investigations further extend into how protein complexes on lipid domains may enable the development of nanoscale transport systems.

Engineering lipid membrane domains for selective protein affinity

245th National Meeting (2013)

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