Preferred conformations and flexibility of aminoacyl side chain of penicillins |
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Authors: | T.K. Vasudevan V.S.R. Ran |
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Affiliation: | Molecular Biophysics Unit; Indian Institute of Science; Bangalore - 560 012; India |
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Abstract: | Possible conformations of penicillin G; d and l isomers of ampicillin; α-amino-α-methyl-benzyl penicillins and 3- pyridyl methyl penicillin have been studied by an energy minimization procedure using empirical potential functions. The preferred conformations of these antibiotics have been correlated with their biological activity. The conformational requirement of the antibiotic to be active against Gram-positive and Gram-negative (β-lactamase-negative) bacterial strains seems to be the same. The reduced activity of penicillin G against Gram-negative bacteria has been attributed to its lower ability to permeate the outer membrane. The flexibility of the sidechains of these antibiotics is also shown to be important for the desired biological activity. |
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Keywords: | Penicillin conformation side chain flexibility β-lactam antibiotics structure-activity relationships |
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