|dc.description.abstract||In eukaryotic cells, membrane spanning proteins are tethered to the lipid bilayer mostly through α-helical transmembrane (TM) domains. These membrane-embedded sequences are capable of interacting with each other, driving both stable and dynamic supramolecular organization of TM proteins. Peptides derived from TM α-helical domains, known as TM peptides, can destabilize TM interactions and, as a result, modulate protein activity. In light of the pivotal role played in the cell by membrane proteins, agents modulating their functions are of great pharmaceutical interest.
In this review we will discuss general design requirements for TM peptides developed for therapeutic applications and present some examples of successful modulation of biologically relevant TM proteins. In addition, promising applications of TM peptides employing their membrane self-insertion properties are presented.||