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دوگانه دوست
Fig. 3.4 Schematic model for altering bilayer physical properties by lipids or small amphiphiles [4].
Membrane association and the lytic activities of cationic amphiphiles are claimed to be governed by hydrophobic interactions with membranes instead.
Cationic amphiphiles are most likely to induce considerable cytotoxic activity by disrupting the bilayer, if not always in a gross manner, perhaps often locally.
In the presence of a hydrophobic bilayer thickness gramicidin A channel length mismatch, τ observed in other studies was mainly seen not to follow the modest change in UgA,gA due to a slight change of the gramicidin A monomer's charge profile in the case of bind- ing of amphiphiles, anti-fusion, or antimicrobial peptides with channels in a varied membrane environment.
The experimental studies [10, 11, 13] claimed to induce increased elasticity into bilayers by bilayer-active amphipathic molecules, such as several anti-fusion peptides, amphiphiles like triton X-100 and capsaicin, and even an antimicrobial peptide gramicidin S.
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