Investigating the role of GXXXG motifs in helical folding and self-association of plasticins, Gly/Leu-rich antimicrobial peptides

Insight into the mechanism of action of temporin-SHa, a new broad-spectrum antiparasitic and antibacterial agent

“…The high number of Gly residues does not appear to be detrimental to helix stability. This is likely linked to the exclusive distribution of Gly over the hydrophilic face, as is also observed for Gly-rich plasticin antimicrobial peptides [58], with helix stabilization promoted by favorable interactions of bulky side chains on the hydrophobic face.…”

Molecular mechanism of synergy between the antimicrobial peptides PGLa and magainin 2

“…In the β strand, the Gly 18 xxxGly 22 motif was only sensitive to large replacements but small replacements did not reduce activity 79 . Plasticins are Gly-rich AMPs from frogs, and in a recent study two of them, plasticin-B1 and plasticin-DA1, were investigated 80 . Both of them have several sequential GxxxG motifs, but no strong self-association was observed 80 .…”

Single‐point mutation‐mediated local amphipathic adjustment dramatically enhances antibacterial activity of a fungal defensin

“…So, it is not surprising to see that the 5 analogs substantially enhanced antibacterial activity in contrast to E8D, as Asp 8 replacement likely rescues the salt bridge to stabilize the c-loop. This reminds us of the linear a-helical AMPs that are often present in an unordered state in aqueous solution but fold into a-helix in a membrane environment (50)(51)(52). In line with those observations, it is generally assumed that the unstructured local subdomain of these enhanced peptides with a flexible c-loop fold into a well-defined amphipathic structure upon binding to the target membrane.…”

“…This reminds us of the linear α‐helical AMPs that are often present in an unordered state in aqueous solution but fold into α‐helix in a membrane environment (50–52). In line with those observations, it is generally assumed that the unstructured local subdomain of these enhanced peptides with a flexible c‐loop fold into a well‐defined amphipathic structure upon binding to the target membrane.…”