Release date: 2014-10-30
Researchers at the University of Bristol in the United Kingdom focus on the role of enzymes in bacteria that break down the structure of antibiotics, stop the action of antibiotics, and make bacteria resistant.
The new findings, published in the journal Chemical Communications, suggest that testing the enzyme's response to certain antibiotics is possible, which will help scientists develop new antibiotics with much lower risk of resistance.
Using a technology developed by a Nobel laureate: QM/MM (Quantum Mechanics/Molecular Mechanics Simulation), the Bristol team was able to gain insight into the antibiotic response of beta-lactamase at the molecular level.
Researchers are particularly interested in understanding the increasingly resistant carbapenems, which are called "the last resort" of antibiotics, which are used against many bacterial infections and infections of super bacteria such as E. coli. Due to resistance to carbapenems, some bacterial infections will not be cured, resulting in mild infections that can become very dangerous and even fatal.
The QM/MM simulation results show that the most important step in the whole process of drug resistance is the antibiotics that have been decomposed by the enzyme 'outside'. If the above process occurs very quickly, the enzyme can continue to break down the antibiotics and the bacteria gain resistance. If it happens slowly, the enzyme does not break down more antibiotics, so the bacteria are more likely to die.
The rate of this "efflux" depends on the level of the energy barrier of the efflux reaction. If the reaction energy barrier is high, the efflux "slowly occurs. If the reaction energy barrier is low, the "outside" will occur more quickly?" .
Professor Adrian Mulholland said: We have shown that computer simulations can be used to determine which enzymes break down and rapidly efflux carbapenems, and which enzymes slowly efflux carbapenem antibiotics.
Source: Bio Valley
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