Abstract
The construction of artificial membrane proteins from first principles is of fundamental interest and holds considerable promise for new biotechnologies. This review considers the potential advantages of adopting a strictly minimalist approach to the process of membrane protein design. As well as the practical benefits of miniaturisation and simplicity for understanding sequence-structure-function relationships, minimalism should also support the abstract conceptualisation of membrane proteins as modular components for synthetic biology. These ideas are illustrated with selected examples that focus upon α-helical membrane proteins, and which demonstrate how such minimalist membrane proteins might be integrated into living biosystems.
Highlights
It is estimated that up to 30% of all proteins are integral membrane proteins [1], with at least one part of the protein sequence passing through a lipid bilayer membrane
We discuss the prospects of designing artificial membrane proteins from scratch — ‘de novo’ — as a particular way to explore the fundamental principles of membrane biology and to realise new applications in synthetic biosystems
There are a large number of protein sequences that have never yet occurred in the natural world
Summary
It is estimated that up to 30% of all proteins are integral membrane proteins [1], with at least one part of the protein sequence passing through a lipid bilayer membrane. The most obvious targets for the minimal design of membrane proteins are transmembrane α-helical bundles, and this will be the focus of the discussion below. This suggests that it will be relatively easy to reduce the complexity of transmembrane segments while retaining secondary structure, and the lipophillic domains of natural helical membrane proteins are already built from a somewhat restricted palette of amino acids.
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