Methicillin resistant Staphylococcus aureus (MRSA) is one of the most prevalent pathogens that account for severe nosocomial infections in millions of patients annually [1]. High resistance to beta-lactam antibiotics exhibited by this organism can be majorly attributed to its ability to produce a class of enzymes called beta-lactamases. Our team investigated the protective effect of a group of charged metallopolymers on antibiotics like penicillin, which are usually hydrolyzed by betalactamases, thus making them ineffective. For this purpose, we employed several biochemical and structural approaches to study interactions of these recombinant enzymes with conjugate complexes of penicillin and metallopolymers in vitro [2]. Recombinant enzymes are often modified in order to improve their expression, yield and structural studies. This study analyzed the effects of different modifications of recombinant beta-lactamases on their stability and activity in vitro. Comparison of enzymatic characteristics and the interactions of modified enzymes with conjugates of penicillin and metallopolymers is discussed.

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