Table 1.

Studies reporting focal interactions between antimicrobial peptides and bacteria.

Authors	Species	Findings
Hasper et al., 2006	Bacillus subtilis and Bacillus megaterium	Nisin disrupted septal and helical distribution of lipid II and aggregated with lipid II in the membrane.
Scherer et al., 2015	Bacillus subtilis	Nisin inhomogeneously bound lipid II, forming aggregates that caused cell death.
Vega and Caparon, 2012	Streptococcus pyogenes	Human neutrophil peptide 1 (HNP-1) and polymyxin B (PxB) disrupted anionic Exportal domain and delocalized the SecA translocase.
Kandaswamy et al., 2013	Enterococcus faecalis	Human β-defensin 2 (hBD2) focally targeted cell surface and delocalized Sortase A (SrtA) and the SecA translocase.
Wenzel et al., 2014	Bacillus subtilis	A 6-amino acid CAMP delocalized the peripheral membrane proteins MurG and cytochrome c.
Zweytick et al., 2014	E. coli	Lactoferricin-derived N-acylated AMPs disrupted phosphatidylethanolamine (PE) and cardiolipin membrane domains and caused defective cell division.
Rangarajan et al., 2013	E. coli	Cecroprin A permeabilized the outer and cytoplasmic membranes in discrete membrane regions.
Tran et al., 2013	Enterococcus faecalis	Daptomycin targeted the division septum.
Pogliano et al., 2012	Bacillus subtilis	Daptomycin delocalized cell division protein DivIVA.
Rangarajan et al., 2013	E. coli	Cecroprin A caused localized permeabilization of the cell membrane