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Review
. 2010 Oct 28;6(10):e1001067.
doi: 10.1371/journal.ppat.1001067.

Antimicrobial peptides: primeval molecules or future drugs?

Brian M Peters  1 , Mark E Shirtliff, Mary Ann Jabra-Rizk
Affiliations
Review

Antimicrobial peptides: primeval molecules or future drugs?

Brian M Peters et al. PLoS Pathog. .
No abstract available

PubMed Disclaimer

Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Figure 1
Figure 1. Protein models representing the structural differences of the four classes of antimicrobial peptides.
Antimicrobial peptides can be grouped into four major classes based on their secondary structures, including the (A) α-helical peptides, (B) peptides composed of a series of β-sheets, (C) peptides that adopt unconventional structures, such as extended helices, and (D) peptides that assemble into loops. All structures were obtained freely from the RCSB Protein Data Bank (PDB) (http://www.pdb.org/) and have been referenced according to their Digital Object Identifier (DOI) . Additional information for each AMP may be obtained by consulting the RCSB PDB and cross-referencing the DOI.
Figure 2
Figure 2. 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.
See this image and copyright information in PMC

References

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