Cytoplasmic membrane disruption

Cytoplasmic membrane disruption Polymyxins Also damage outer membrane of Gram-negative bacteria... 

The current understanding on activation of Tec kinases fits into a two-step model. In the first step an intramolecular interaction between the SH3 domain and aproline-rich region in the TH domain is disrupted by binding ofthe PH domain to phosphoinositides, G protein subunits, or the FERM domain of Fak. These interactions lead to conformational changes of Tec and translocation to the cytoplasmic membrane where, in a second step, Src kinases phosphorylate a conserved tyrosine residue in the catalytic domain thereby increasing Tec kinase activity. Autophosphorylation of a tyrosine residue in the SH3 domain further prevents the inhibitory intramolecular interaction resulting in a robust Tec kinase activation. 

Cytoplasmic membrane Polymyxins Polyenes Imidazoles and triazoles Naftidine Disrupt bacterial membranes Disrupt fungal membranes Inhibit ergosterol synthesis Inhibits ergosterol synthesis Bind to LPS and phospholipids Bind preferentially to ergosterol Pathway not in mammalian cells Pathway not in mammalian cells... 

The answer is c. (Hardman, pp 1143-1144.) Bacitracin, cycloserine, cephalothin, and vancomycin inhibit cell-wall synthesis and produce bacteria that are susceptible to environmental conditions. Polymyxins disrupt the structural integrity of the cytoplasmic membranes by acting as cationic detergents. On contact with the drug, the permeability of the membrane changes. Polymyxin is often applied in a mixture with bacitracin and/or neomycin for synergistic effects. 

After administration of mercuric chloride to adult rat kidneys, several changes were found, for example, pars recta of the proximal tubular segment showing fragmentation and disruption of the plasma membrane, basophilic staining, vesiculation and disruption of endoplasmic reticulum and other cytoplasmic membranes, mitochondrial swelling, loss of mitochondrial dense granules and condensation of nuclear chromatin [223-225]. 

It is bactericidal drug and exerts its action by combining with bacterial ribosome and induces misreading of mRNA codons. Also in sensitive bacteria, disruption of cytoplasmic membrane occurs resulting in leakage of amino acids, ions, leading to bacterial death. 

Assembly and release. The assembly of the capsid and its association with nucleic acid is then followed by release of the virus front the cell. This may occur in different ways, depending upon the nature of the virus. Naked viruses may be released slowly and extruded without cell lysis, or released rapidly by disruption of the cell membrane. DNA viruses, which mature in the nucleus, tend to accumulate within infected cells over a long period. Enveloped viruses generally acquire their envelope and leave the cell by budding through the nuclear or cytoplasmic membrane at a point where virus-specified proteins have been inserted. The budding process is compatible with cell survival. 

Most results on calcium transport have been obtained using cytoplasmic membrane vesicles, which may be prepared in inside-out or right-side-out configurations. Inside-out vesicles may be obtained by the disruption of E. coli cells in a French press. These then accumulate Ca2+ in an energy-dependent fashion, provided ATP or an oxidizable substrate is available. Addition of phosphate enhances the uptake of calcium as calcium phosphate is precipitated inside the tell, thus accounting for the lack of exchangeability of the calcium.186... 

Due to their lipophilicity, organotins are membrane-active and the cytoplasmic membrane is an obvious target of action. Disruption of membrane integrity may occur because of organotin binding or insertion into the membrane. Organotins can also act intra-cellularly and intact organelles may be disrupted. ... 

Organic acids (lactic, acetic) Bacteriocins co2 Hydrogen peroxide Diacetyl Reuterin Ethanol Increase acidity, antimicrobial compounds Nisin only bacteriocin permitted as food preservative, disrupts cytoplasmic membrane Reduces membrane permeability Oxidizes proteins Interacts with arginine-binding proteins Not confirmed, may interact with thiol group in proteins that may lead to oxidative stress (Whitehead et al., 2008)... 

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