| Summary: | 碩士 === 國立中正大學 === 化學研究所 === 92 === As the most widespread resistance mechanism to antibiotics, -lactamases readily and efficiently hydrolyze -lactam rings that effectively inactivate the inhibitory function of the -lactam antibiotics, such as the penicillians and the cephalosporins. Over forty structurally different -lactam compounds are available in more than seventy formulations and the majority of them are currently prescribed for medical use in hospitals. -Lactam antibiotics are well tolerated by humans with, amazingly, few side effects. They interact specifically with their bacterial target, the DD-peptidase. The outstanding number of -lactamases produced by bacteria represents a serious threat to the clinical utility of -lactams. The discovery of -lactamase inhibitors was thought to solve, in part at least, the problem of resistance. Unfortunately, bacteria have evolved new mechanisms of resistance to overcome the inhibitory effects of -lactamase inactivators. In this report, we summarize the diversified mechanistic features of -lactamases interactions with mechanism-based inhibitors. A brief historical overview of the strategies developed to counteract -lactamases is presented followed by a short description of the chemical events which lead to the inactivation of -lactamases by inhibitors. Finally, an update on new development of -lactamase inhibitor protein-II (BLIP-II), light-inactivated antibiotic, and NB2001 antibacterial agent is discussed.
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