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Updated: Aug 21, 2026

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
Published on: July 28, 2022
De novo design of defined helical bundles in membrane environments
Basar Bilgiçer1, Krishna Kumar
1Department of Chemistry, Tufts University, Medford, MA 02155, USA.
Abstract:
Control of structure and function in membrane proteins remains a formidable challenge. We report here a new design paradigm for the self-assembly of protein components in the context of nonpolar environments of biological membranes. An incrementally staged assembly process relying on the unique properties of fluorinated amino acids was used to drive transmembrane helix-helix interactions. In the first step, hydrophobic peptides partitioned into micellar lipids. Subsequent phase separation of simultaneously hydrophobic and lipophobic fluorinated helical surfaces fueled spontaneous self-assembly of higher order oligomers. The creation of these ordered transmembrane protein ensembles is supported by gel electrophoresis, circular dichroism spectroscopy, equilibrium analytical ultracentrifugation, and fluorescence resonance energy transfer.
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