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Chapter 5 : Antibiotics That Disrupt Membrane Integrity

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Antibiotics That Disrupt Membrane Integrity, Page 1 of 2

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Abstract:

It has been known for decades that agents that can disrupt the integrity of bacterial membranes are bactericidal. Antiseptic chemicals that act as germicides and sanitizers kill bacteria and other microbes quickly when used, for example, in hand washing. Active ingredients include organic aliphatic alcohols and phenols, as well as aldehydes, acting as solvents to dissolve membranes (McDonnell and Russell, 2001). Disinfectants for microbes on inorganic surfaces can also contain oxidizing agents such as hydrogen peroxide or iodine solutions that also kill rapidly. These agents do not have enough selectivity for bacterial membranes over eukaryotic, human cell membranes to have a sufficient therapeutic index to be used systemically and so are restricted to topical use.

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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Figures

Image of Figure 5.0
Figure 5.0

Schematic for oligomerization of Ca-daptomycin complexes and insertion into bacterial membranes, leading to depolarization.

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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Image of Figure 5.1
Figure 5.1

Human defensins are disulfide-rich small proteins that kill bacteria by insertion and selective accumulation in bacterial membranes. Defensins are produced in many different tissues as key components of innate immune responses. (Image reprinted from Huttner and Bevins [1999] with permission and all peptides are defined therein.)

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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Image of Figure 5.2
Figure 5.2

Three limiting models for insertion of cationic peptides into anionic phospholipid membranes. Initial interaction of helical peptide with membrane head groups. (a) Insertion in three modes: (b) barrel stave, (c) toroidal pores, and (d) carpet. (Adapted from Brogden [2005] with permission.)

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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Image of Figure 5.3
Figure 5.3

(a) Structure of human β-defensin 2 (hBD2). (b) Distribution of hBD2 and -3 in normal oral epithelium. (Panel b reprinted from Weinberg et al. [2012] with permission.)

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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Image of Vignette 5.1
Vignette 5.1

Nuclear magnetic resonance (NMR) solution structure of cathelicidin LL-37 (PDB 2K6O) with electrostatic map generated using PyMOL. As with most helical AMPs, distinct charged hydrophilic (blue/red portions of helix) and uncharged hydrophobic (gray) regions are observed. This amphipathic nature empowers these “carpet bombers” to disrupt membranes (Wang, 2008).

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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Image of Figure 5.4
Figure 5.4

Physical entrapment of bacteria (purple) in the nanowork of aggregated HD6 (green). (Reprinted from Chu et al. [2012], courtesy of Hiutung Chu and Charles Bevins.)

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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Image of Figure 5.5
Figure 5.5

(a) Microbisporicin, a posttranslationally modified lantipeptide, disrupts membranes subsequent to lipid II binding. (b) Posttranslationally modified amino acids found in microbisporicin and analogs (Foulston and Bibb, 2012).

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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Image of Figure 5.6
Figure 5.6

Structures of surfactin (a) and daptomycin (b), nonribosomal lipopeptidolactones. The acyl lipid chains are in red and the lactones highlighted in yellow. (c) Structure of polymyxin E with lipid chain in red and cationic amine side chains in blue. (d) Structure of teicoplanin, a lipoglycopeptide.

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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Image of Vignette 5.2
Vignette 5.2

The skin of the African clawed frog contains antimicrobial peptides (AMPs) including the helical peptide magainin. Replacement of terminal leucine residues with hexafluoro-leucines generates fluorogainin-1. (Reprinted from Gottler et al. [2008] with permission.)

Citation: Walsh C, Wencewicz T. 2016. Antibiotics That Disrupt Membrane Integrity, p 102-113. In Antibiotics: Challenges, Mechanisms, Opportunities. ASM Press, Washington, DC. doi: 10.1128/9781555819316.ch5
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