Sandbox Reserved 429
From Proteopedia
(Difference between revisions)
| Line 13: | Line 13: | ||
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). | 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). | ||
The goal of a chemist is to develop a way to break this cell wall, thus destroying the bacteria. To achieve this, the penicillin is introduced to the bacteria and then reacts with PBPs (using β-lactam ring), preventing it from forming 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 β-lactamase 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 goal of a chemist is to develop a way to break this cell wall, thus destroying the bacteria. To achieve this, the penicillin is introduced to the bacteria and then reacts with PBPs (using β-lactam ring), preventing it from forming 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 β-lactamase 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 <scene name='48/483886/ | + | The complex of the PBP with <scene name='48/483886/Phenoxy/2'>Phenoxylactivicin</scene> is shown on the picture. |
Picture on the left is displayed as N-terminus to C-termiunus Rainbow for PBP complex. The coloring goes as shown on the sample: | Picture on the left is displayed as N-terminus to C-termiunus Rainbow for PBP complex. The coloring goes as shown on the sample: | ||
<blockquote> | <blockquote> | ||
Revision as of 16:59, 23 March 2016
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
Penicillin binding protein/lactivicin (inhibitor) (2jch)[1]
by Tyler Carpenter, Samuel Pierce, Hyunjoon Choi, Anton El Khoury and Tiankai Zhang
Student Projects for UMass Chemistry 423 Spring 2016
| |||||||||||
