Figures & data
Figure 1. Molecular models of AMPs structures. These models are from the NMR structural database. (A) The amphipatic α-helical structure of magainin 2 (PDB code 2MAG). (B) Two-standed antiparalel β-sheet of protegnin-1 (PDB code 1PG1). (C) The β-turn loop structure of a cyclic indolidin peptide derivate (PDB code 1QX9). (D) Structure of indolicidin bound to dodecyphospholidine micelles shows the random coil structure (PDB code 1G89). Reused with permission, first published by Huang et al. [Citation3].
![Figure 1. Molecular models of AMPs structures. These models are from the NMR structural database. (A) The amphipatic α-helical structure of magainin 2 (PDB code 2MAG). (B) Two-standed antiparalel β-sheet of protegnin-1 (PDB code 1PG1). (C) The β-turn loop structure of a cyclic indolidin peptide derivate (PDB code 1QX9). (D) Structure of indolicidin bound to dodecyphospholidine micelles shows the random coil structure (PDB code 1G89). Reused with permission, first published by Huang et al. [Citation3].](/cms/asset/98e707cb-f442-4267-91a4-f9a4972cbe78/tbeq_a_1611385_f0001_c.jpg)
Table 1. Reprezentative antimicrobial peptides, shown by Sbanca Dorica-Mirelaa and Jianu Ionela [Citation4]
Figure 2. Primary structures of the human α- and β-defensins. The disulphide bond connectivity is indicated with lines, published by Wiesner and Vilcinskas [Citation15].
![Figure 2. Primary structures of the human α- and β-defensins. The disulphide bond connectivity is indicated with lines, published by Wiesner and Vilcinskas [Citation15].](/cms/asset/29632f6f-4e89-47be-ae42-d0e4e0442faa/tbeq_a_1611385_f0002_b.jpg)
Table 2. Distribution of human antimicrobial peptides. Reused with permission, originally given by Cole and Ganz [Citation25].
Figure 3. The proposed diverse mechanistic modes of action for antimicrobial peptides in microbial cells. (A) Disruption of cell membrane integrity: (1) random insertion into the membrane, (2) alignment of hydrophobic sequences, and (3) removal of membrane sections and formation of pores. (B) Inhibition of DNA synthesis. (C) Blocking of RNA synthesis. (D) Inhibition of enzymes necessary for linking of cell wall structural proteins. (E) Inhibition of ribosomal function and protein synthesis. (F) Blocking of chaperone proteins necessary for proper folding of proteins. (G) Targeting of mitochondria: (1) inhibition of cellular respiration and induction of ROS formation and (2) disruption of mitochondrial cell membrane integrity and efflux of ATP and NADH, given by Peters et al. [Citation59].
![Figure 3. The proposed diverse mechanistic modes of action for antimicrobial peptides in microbial cells. (A) Disruption of cell membrane integrity: (1) random insertion into the membrane, (2) alignment of hydrophobic sequences, and (3) removal of membrane sections and formation of pores. (B) Inhibition of DNA synthesis. (C) Blocking of RNA synthesis. (D) Inhibition of enzymes necessary for linking of cell wall structural proteins. (E) Inhibition of ribosomal function and protein synthesis. (F) Blocking of chaperone proteins necessary for proper folding of proteins. (G) Targeting of mitochondria: (1) inhibition of cellular respiration and induction of ROS formation and (2) disruption of mitochondrial cell membrane integrity and efflux of ATP and NADH, given by Peters et al. [Citation59].](/cms/asset/1add5fc0-6e79-4580-9c17-d5f3c8ae8a15/tbeq_a_1611385_f0003_c.jpg)
Table 3. Some examples of AMP formulations given by Carmona-Ribeiro and de Melo Carrasco [Citation77].