Medicinal Chemistry–III. Main Lectures Presented at the by P. Pratesi

By P. Pratesi

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O n the contrary, a screening directed against the target enzyme, the bacterial R N A polymerase, would select such derivatives, leaving to the medicinal chemist the possibility of modifying their structure in order to increase their permeability through the cell wall. Also rifamycin Β belongs to this group ; but although inactive per se, it is easily transformed into rifamycin S, which is very active, and only as a result of this unusual property has not been 55 neglected . Table 4. Relationship between inhibition of bacterial growth and of bacterial R N A polymerase Class Activity of rifamycins on bacterial cells 1 Most active rifamycins 2 Most inactive rifamycins 3 Rifamycins unable to cross the bacterial cell wall 4 Rifamycins which undergo structural modification during antibacterial test 395 on bacterial R N A polymerase + + — + + — — — P.

Greco, R. Ballotta and P. Sensi, Farmaco (Pavia) Ed. Sei. 16, 755 (1961). P. Sensi, M. T. Timbal and A. M. Greco, Antibiot. Chemotherapy, 12, 488 (1962). R. Cricchio and G. Tamborini, J. Med. Chem. 14, 721 (1971). G. G. Gallo, C. R. Pasqualucci, N . Maggi, R. Ballotta and P. Sensi, Farmaco (Pavia) Ed. Sei. 21, 68 (1966). Ν. Maggi, V. Arioli and G. Tamborini, Farmaco (Pavia) Ed. Sei. 24, 263 (1969). N . Maggi and R. Pallanza, Farmaco (Pavia) Ed. Pr. 22, 307 (1967). N . Maggi, V. Arioli and P. Sensi, J.

Ballotta, S. Furesz, R. Pallanza and V. Arioli, J. Med. Chem. 7,596 (1964). A. M. Greco, R. Ballotta and P. Sensi, Farmaco (Pavia) Ed. Sei. 16, 755 (1961). P. Sensi, M. T. Timbal and A. M. Greco, Antibiot. Chemotherapy, 12, 488 (1962). R. Cricchio and G. Tamborini, J. Med. Chem. 14, 721 (1971). G. G. Gallo, C. R. Pasqualucci, N . Maggi, R. Ballotta and P. Sensi, Farmaco (Pavia) Ed. Sei. 21, 68 (1966). Ν. Maggi, V. Arioli and G. Tamborini, Farmaco (Pavia) Ed. Sei. 24, 263 (1969). N . Maggi and R.

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