Penicillin-binding Proteins.docVIP

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Penicillin-binding Proteins

 PAGE \* MERGEFORMAT 11 Penicillin-binding Proteins Penicillin-binding proteins (PBPs) are widely present in bacteria the surface of a membrane protein, is within the phthalocyanine amine β _ the primary role of antibiotic target site. Different bacteria types and levels vary. However, there are a number of various strains of the PBPs of similar structure and function of the bacterial growth and reproduction play an important role. PBPs structure and amount of change produced an important mechanism of bacterial resistance. Today, although a wide range of types of antibiotics, but in the treatment of resistant bacteria is still a lack of effective tools. Therefore, in recent years, carried out around the PBPs a lot of research work, trying to understand molecular structure and gene level PBPs, to explore mechanisms for bacterial resistance to antibiotics in an attempt to get more effective treatment. 1 PBPs research history and basic concepts Despite the very early clinical application of penicillin, but by the 20th century, 50 years, been recognized as penicillin, by interfering with the surface structures of bacteria play a role. 60 years, the structure of bacterial cell wall has been clarified for people to understand the mechanism of penicillin and PBPs basis. 1972 Suginak. Blumberg, and Stro minge: discovery of penicillin-binding protein, using radioisotope labeled penicillin can be marked bacterial surface PBPs, but later studies have found that not all the role of PBP were the fatal penicillin target site. All bacteria contain a variety of penicillin-binding proteins, PBPs of different genus of its content, different types, different antibiotics with a different combination of the PBP proteins have different antimicrobial activity. Thus, PBP combination with different combination of antibiotics, often resulting synergies. Each strain has a set of specific PBPs, said PBPs spectrum. In a strain in the PBPs by molecular size of the order, respectively, s

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