Introduction
Every bacteria wants to live. Every bacteria wants to reproduce. To achieve both, bacteria need some sort of protection that will maintain the structure inside and will protect it from outside dangers. This protection is called cell wall, that primarily consists of a polymer that is called peptidoglycan. This compound can be synthesized only with the help of penicillin binding proteins (PBPs) , which are the target of this article (the name basically comes from a way it was discovered). PBP serves as a catalyst in the final stages of peptidoglycan synthesis, transglycosylation and transpeptidation in particular.[2] Although there are multiple types of PBPs, they all bind penicillin (however, with different affinities) and this is what is important for this article.
As the bacteria infiltrates the organism, it becomes necessary to somehow destroy it. One way is to to break this cell wall. To achieve this, the penicillin is introduced to the bacteria that later reacts with PBPs (using β-lactam ring ), preventing it from catalyzing the formation of a peptidoglycan and, as a result, stops the formation of a cell wall. However, many pathogenic bacteria have evolved a way to mutate themselves to be immune to various drugs that contain this β-lactam rings. What happens is that bacterium produces enzyme, called that cleaves the β-lactam ring on a penicillin and thus preventing it from reacting with PBPs. To solve this problem, the new drug, called, lactivicin was developed that contains gamma-lactone rings and cycloserine as substitutions to β-lactam. So far, it has proved to be an efficient antibiotic. It successfully binds to PBPs and prevents cell wall from forming.
Recently, an analog of lactivicin, phenoxylactivicin (PLTV) was developed and is discussed in this article.
The complex of the PBP with is shown on the picture.
Picture on the right is displayed as N-terminus to C-termiunus Rainbow for. The coloring goes as shown on the sample:
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Carboxy Terminus |
Overall Structure
Penicillin Binding Proteins have specific structures and designs that promote allow the binding of Penicillin and other antibiotics. One of the enzymes within the PBP family is . This enzyme is responsible for the link between two chains in the peptidoglycan network [3]
