Aminoglycosides, chemistry resistance

A semisynthetic aminoglycoside whose design was also based on knowledge of resistance chemistry is the C-l-N-ethylsisomicin, netilimicin. This alkylation protects the drug against ANT (2") and AAC(3)I. 

John S. Blanchard received his BS in chemistry from Lake Forest College and obtained his Ph.D. from the laboratory of W. W. Cleland at the University of Wisconsin. After a 3-year NIH-sponsored postdoctoral fellowship, he was appointed assistant professor of biochemistry at the Albert Einstein College of Medicine in New York City in 1983. In 1998, he became the Dan Danciger Professor of Biochemistry. His early research interests focused on the determination of kinetic isotope effects exhibited by flavin-containing enzymes. His collaborative studies on the mechanism of action, and resistance, to isoniazid in Mycobacterium tuberculosis led to his current interests in antibiotic resistance. His present interests include the structure and function of essential biosynthetic enzymes in M. tuberculosis, resistance to aminoglycosides and fluoroquinolones, and proteome-wide identification of acetylated proteins. He is the author of over 140 research papers and 20 reviews and has been awarded seven United States patents. His work has been generously supported by the United States National Institutes of Health for the last 24 years. 

The mechanisms of inactivation of aminoglycoside antibiotics by resistant organisms, and die chemistry of the inactivated products, are described in Chapter 4 of this Volume (see p. 183). 

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