Abstract
Gramicidin is a potent modulator of long-range membrane lipid organization and therefore a useful model to understand aspects of lipid polymorphism in relation to the structure and function of biological membranes. In this article we will review the peptide’s lipid structure-modulating activity in relation to recent studies on the lipid flip-flop enhancing ability of gramicidin in erythrocyte membranes. Special emphasis will be placed on the essential role of the conformation of gramicidin and its aggregational behavior in these events. The relationships between the other known properties of gramicidin, e.g., channel formation and involvement of gene regulation, are indicated. It is suggested that the unique concentration of the four tryptophans towards the C-terminus is the structural link between these different functional properties of the peptide.
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