1.C.76 The Pore-forming Maculatin Peptide (Maculatin) Family

Maculatins exist in four isoforms (1.1, 1.2, 2.1 and 3.1). They form pores in lipid bilayers (Ambroggio et al., 2005). Each of these small peptides consists of a single α-helical TMS per polypeptide chain which oligomerize to produce pores in biological membranes. These can cause leakage and thus kill the cell.

Maculatin forms an ensemble of structurally diverse temporarily functional low-oligomeric pores, which mimic integral membrane protein channels in structure (Wang et al. 2016). These pores continuously form and dissociate in the membrane. Membrane permeabilization is dominated by hexa-, hepta- and octamers, which conduct water, ions and small dyes. Pores form by consecutive addition of individual helices to a transmembrane helix or helix bundle. The diversity of the pore architectures-formed by a single sequence-may be a key feature in preventing bacterial resistance and could explain why sequence-function relationships in AMPs remain elusive (Wang et al. 2016).

Peptides, indolicidin, aurein 1.2, magainin II, cecropin A and LL-37 all cause a general acceleration of essential lipid transport processes without altering the overall structure of the lipid membranes or creating organized pore-like structures (Nielsen et al. 2020). Rapid scrambling of the lipid composition associated with enhanced lipid tNielsen et al. 2020). Rapid scrambling of the lipid composition associated with enhanced lipid transport may trigger lethal signaling processes and enhance ion transport.