Aminosicillin is a widely used β-neamide antibiotics whose mechanisms of action are based on interference with the synthesis of bacterial cell walls, which, through a series of complex and sophisticated molecular processes, achieves effective inhibition of bacteria ‘ growth and reproduction, ultimately for the purpose of microbicide or antibicide.
Bacteria cell walls are a key barrier to the integrity of bacterial cell formations and structures, which not only give bacteria specific shapes, but also protect cells from adverse factors such as changes in external osmosis pressure. The main component of the cell wall is aluminum chorus, a large molecular polymer that is conjunctivated by a combination of sugar chains and short beryllium, and the synthesis process involves multiple steps and the involvement of numerous enzymes.
At the final stage of the synthesis of pelicans, there are some key enzymes known as penicillin integrator proteins (PBPs). These PBPs have multiple functions, the most important of which is to catalyze the conjunctive reaction between the pelican sugar chains and to make the cell wall a solid and stable web structure.
The chemical structure of ammonia silin contains a unique β-neamide ring, which is at the core of its antibacterial activity. When it enters the bacteria’ environment, it is able to identify and integrate accurately the PBPs active position on the bacterial membrane, based on its own chemical structure properties. The combination has a high degree of specificity and affinity, as if the key and lock were accurately matched.
Once the ammonia silin is successfully integrated with PBPs, a series of chain reactions can be triggered, resulting in the normal enzyme activity of the PBPs being inhibited. Since PBPs play an indispensable catalytic role in the pelican conjunctivation, the process of synthesis of pelican is immediately disrupted when its activity is inhibited. The newly created pelican polymal chain is not properly interconnected and the construction of cell walls cannot be successfully completed.
As bacteria grow and breed, the need for a complete cell wall becomes more pressing, but the lack of cell walls is exacerbated by the continued disturbance of ammonia silin. In this case, the balance between the relatively high permeability pressure within the bacteria and the external environment was broken. As a result of the loss of effective support and protection of the cell wall, bacterial cells began to inflate as an over-inflated balloon under internal permeation pressure.
This process of expansion is irreversible and, over time, it has gradually exceeded the limits of the bacterial cellular membranes, resulting in the rupture of the bacterial membranes, the release of cell contents and the death of bacteria. This is the whole process of the action of ammonia sicillin by inhibiting the synthesis of bacterial cytowalls, which in turn causes bacterial death.
It is worth noting that ammonia sielling has a certain level of antibacterial activity for both the Gyran positive and the Gyran cactus, but that there are differences in the cytowall structure of both, which makes it slightly different in the process. The cytex glycol layer of the gland positive fungus is thicker and accounts for a high proportion of stem weight of the cell wall, so that ammonia silin can play a more direct role in the process of synthesis of cytex, causing significant damage to its cell wall structure. The cytowall structure of the gland cactus is relatively complex, with an outer membrane in addition to the thinr permafrost layer. A ammonia silin needs to penetrate the outer membrane before it can be combined with the PBPs on the membrane, which in turn inhibits the synthesis of americ sugar. Despite this additional step, ammonia sicillin is still able to produce effective antibacterial effects on many glucose cactus.
However, during the long-term evolution of bacteria, a number of mechanisms have been developed to deal with the effects of aminosicillin, the most important of which is the production of β-NEA. This enzyme is uniquely identifiable and hydrolysed by the β-neamide ring in aminos, which deprives them of the ability to combine with PBPs and thus to function as antibacterial. This is also one of the major causes of the resistance of ammonia silin. In order to overcome this problem, in clinical treatment, a combination of drug-based strategies is often used to co-use ammonia sicillin with β-neamide inhibitors in order to enhance the antibacterial effects of ammonia sillin, expand its antibacterial spectrum and ensure effective treatment of infection.
