Ординатура / Хирургия / Библиотека им академика М.И. Перельмана / Книга_5663_Библиотеки_им_академика_М_И_Перельмана

contains some polar amino acids more than melittin at the N-terminal end that are eliminated by a protease after translation [9]. These polar amino acids at this end ensure that this toxic peptide is never present during its translation into the ribosomes [10]. The main reason for this is that the N-terminal region of melittin is predominantly hydrophobic while the carboxy-terminal region is hydrophilic due to the presence of a stretch of positively charged amino acid [ ], leading to an 7 amphipath that allows it to interact with the biological membranes [11]. Melittin has diverse biological and pharmacological activities [12], in particular the abil­ity to modify the functions of the immune system in the body [13]. It has been seen that the addition of melittin to bacteria increases the turgor pressure of the cells followed by a decrease in the cell pressure, which could destroy the cellular envelope and could be the reason for cell lysis and its antimicrobial properties [14]. In human erythrocytes, melittin binds rapidly to its membrane and forms pores leading to an alteration of the permeability that causes the release of hemoglobin to the extracellular medium, and this causes the hemolysis at room temperature [7]. It also has the capacity to affect the dynamics of membrane proteins, causing their aggregation and immobilizing them in the plane of the lipid bilayer [15] and acting as a potent inhibitor of Ca2+ATPase, H+K+ATPase, Na+K+ATPase, and protein kinase (Figure ) [7].