Bacterial membranes modification

Among the long-chain proline-rich AMPs, diptericin that is carrying post-translational modifications (C-terminal amidation and two O-glycosylations, see for details the previous section of this chapter) has a controversial mode of action. It was shown to disrupt the bacterial membrane, but it is unlikely that it acts primarily as a pore-former, rather it is expected to target metabolic processes such as nucleic acid, protein, and cell wall synthesis [98]. 

Another method used to vary the AG° of the recombination reaction without chemical modification of the centers, consists of placing the system in an electric field whose orientation and intensity are well defined [141]. However, the energy level shifts induced by the field also change the electronic factors, so that the interpretation of the experimental results is not straightforward. Bixon and Jortner have proposed using electric field effects to elucidate the nature of the primary electron step in bacterial photosystems [142], a problem that will be discussed in Sect. 3.5. One basic difficulty encountered in this method is the evaluation of the internal field effectively seen by the redox centers in the membrane. 

The aminoglycosides interfere with bacterial protein synthesis by binding irreversibly to ribosome and could cause cell membrane damage. They may be inactivated by bacterial resistant enzymes but bacteria could also display resistance through ribosomal modifications or by decreased uptake of antibiotic into the bacterial cell. 

In a similar way, a well-adhered surface modification of BC fibers can be achieved with Ti(>2 nanoparticles (with a diameter of about 10 nm) by the hydrolysis of titanium tetraisopropanolate adsorbed onto the fibers. It was observed that the titania-coated surface appears to be dense and have low porosity and to consist of near-spherical grains. By washing with sodium carbonate solution, the TiC>2 films were not removed during neutralization. It seems that the particles have formed strong interactions with BC. The coated membranes showed substantial bactericidal properties under UV radiation and white light (containing a small fraction of UV) conditions, too. This effect is caused by the photocatalytic destruction of the bacterial cells. 

G-protein a-subunits also possess specific residues that can be covalently modified by bacterial toxins. Cholera toxin catalyzes the transfer of ADP-ribose moiety of NAD to a specific arginine residue in certain a-subunits, whereas pertussis toxin ADP-ribosylates those a-subunits that contain a specific cysteine residue near the carboxy-terminus. Modification of the a-subunit by cholera toxin persistently activates these protein by inhibiting their GTPase activity, whereas pertussis toxin inactives Gia protein and thereby results in the uncoupling of receptor from the effector. G-protein a-subunits are regulated by covalent modifications by fatty acids myristate and palmate. These lipid modifications serve to anchor the subunits to the membrane and increase the interaction with other protein and also increase the affinity of the a-subunit for 3y. In this regard, the myristoylation of Gia is required for adenylyl cyclase inhibition in cell-free assay (Taussig et al. 1993). 

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